ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Histone-lysine N-methyltransferase SETMAR

Intramolecular
Cysteine 75 and cysteine 87
Cysteine 75 and cysteine 122
Cysteine 289 and cysteine 294
Cysteine 75 and cysteine 77
Cysteine 75 and cysteine 82
Cysteine 287 and cysteine 289
Cysteine 287 and cysteine 294
Cysteine 82 and cysteine 124
Cysteine 77 and cysteine 87
Cysteine 82 and cysteine 87
More...
Cysteine 75 and cysteine 124
Cysteine 75 and cysteine 89
Cysteine 226 and cysteine 289
Cysteine 226 and cysteine 294
Cysteine 75 and cysteine 118
Cysteine 124 and cysteine 128
Cysteine 77 and cysteine 82
Cysteine 118 and cysteine 124
Cysteine 89 and cysteine 122
Cysteine 87 and cysteine 89
Cysteine 122 and cysteine 124
Cysteine 87 and cysteine 118
Cysteine 226 and cysteine 287
Cysteine 118 and cysteine 122
Cysteine 82 and cysteine 128
Cysteine 75 and cysteine 128
Cysteine 87 and cysteine 122
Cysteine 87 and cysteine 124
Cysteine 82 and cysteine 118
Cysteine 77 and cysteine 124
Cysteine 87 and cysteine 128
Cysteine 82 and cysteine 122
Cysteine 89 and cysteine 124
Cysteine 118 and cysteine 128
Cysteine 77 and cysteine 122
Cysteine 77 and cysteine 118
Cysteine 77 and cysteine 89
Cysteine 122 and cysteine 128
Cysteine 82 and cysteine 89
Cysteine 77 and cysteine 128
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 75 and 87 (61 and 73 respectively in this structure).

Details

Redox score ?
88
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
5
% buried
37
Peptide accession
Q53H47
Residue number A
75
Residue number B
87
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 75 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 87 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 75 and 122 (61 and 108 respectively in this structure).

Details

Redox score ?
88
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
5
% buried
40
Peptide accession
Q53H47
Residue number A
75
Residue number B
122
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 75 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 122 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 289 and 294 (275 and 280 respectively in this structure).

Details

Redox score ?
88
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
20
Peptide accession
Q53H47
Residue number A
289
Residue number B
294
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 289 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 294 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 75 and 77 (61 and 63 respectively in this structure).

Details

Redox score ?
87
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
5
% buried
22
Peptide accession
Q53H47
Residue number A
75
Residue number B
77
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 75 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 77 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 75 and 82 (61 and 68 respectively in this structure).

Details

Redox score ?
87
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
5
% buried
34
Peptide accession
Q53H47
Residue number A
75
Residue number B
82
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 75 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 82 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 287 and 289 (273 and 275 respectively in this structure).

Details

Redox score ?
86
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
6
% buried
40
Peptide accession
Q53H47
Residue number A
287
Residue number B
289
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 287 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 289 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 287 and 294 (273 and 280 respectively in this structure).

Details

Redox score ?
86
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
26
Peptide accession
Q53H47
Residue number A
287
Residue number B
294
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 287 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 294 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 82 and 124 (68 and 110 respectively in this structure).

Details

Redox score ?
83
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
36
Peptide accession
Q53H47
Residue number A
82
Residue number B
124
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 82 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 124 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 77 and 87 (63 and 73 respectively in this structure).

Details

Redox score ?
83
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
24
Peptide accession
Q53H47
Residue number A
77
Residue number B
87
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 77 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 87 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 82 and 87 (68 and 73 respectively in this structure).

Details

Redox score ?
83
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
38
Peptide accession
Q53H47
Residue number A
82
Residue number B
87
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 82 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 87 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 75 and 124 (61 and 110 respectively in this structure).

Details

Redox score ?
83
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
60
Minimum pKa ?
5
% buried
36
Peptide accession
Q53H47
Residue number A
75
Residue number B
124
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 75 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 124 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 75 and 89 (61 and 75 respectively in this structure).

Details

Redox score ?
83
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
5
% buried
44
Peptide accession
Q53H47
Residue number A
75
Residue number B
89
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 75 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 89 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 226 and 289 (212 and 275 respectively in this structure).

Details

Redox score ?
82
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
6
% buried
32
Peptide accession
Q53H47
Residue number A
226
Residue number B
289
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 226 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 289 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 226 and 294 (212 and 280 respectively in this structure).

Details

Redox score ?
82
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
18
Peptide accession
Q53H47
Residue number A
226
Residue number B
294
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 226 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 294 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 75 and 118 (61 and 104 respectively in this structure).

Details

Redox score ?
81
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
5
% buried
nan
Peptide accession
Q53H47
Residue number A
75
Residue number B
118
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 75 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 118 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 124 and 128 (110 and 114 respectively in this structure).

Details

Redox score ?
80
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
8
% buried
44
Peptide accession
Q53H47
Residue number A
124
Residue number B
128
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 124 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 128 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 77 and 82 (63 and 68 respectively in this structure).

Details

Redox score ?
79
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
22
Peptide accession
Q53H47
Residue number A
77
Residue number B
82
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 77 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 82 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 118 and 124 (104 and 110 respectively in this structure).

Details

Redox score ?
79
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
8
% buried
nan
Peptide accession
Q53H47
Residue number A
118
Residue number B
124
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 118 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 124 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 89 and 122 (75 and 108 respectively in this structure).

Details

Redox score ?
77
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
50
Peptide accession
Q53H47
Residue number A
89
Residue number B
122
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 89 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 122 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 87 and 89 (73 and 75 respectively in this structure).

Details

Redox score ?
77
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
8
% buried
47
Peptide accession
Q53H47
Residue number A
87
Residue number B
89
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 87 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 89 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 122 and 124 (108 and 110 respectively in this structure).

Details

Redox score ?
77
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
42
Peptide accession
Q53H47
Residue number A
122
Residue number B
124
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 122 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 124 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 87 and 118 (73 and 104 respectively in this structure).

Details

Redox score ?
75
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
nan
Peptide accession
Q53H47
Residue number A
87
Residue number B
118
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 87 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 118 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 226 and 287 (212 and 273 respectively in this structure).

Details

Redox score ?
75
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
38
Peptide accession
Q53H47
Residue number A
226
Residue number B
287
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 226 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 287 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 118 and 122 (104 and 108 respectively in this structure).

Details

Redox score ?
74
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
9
% buried
nan
Peptide accession
Q53H47
Residue number A
118
Residue number B
122
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 118 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 122 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 82 and 128 (68 and 114 respectively in this structure).

Details

Redox score ?
71
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
12
% buried
43
Peptide accession
Q53H47
Residue number A
82
Residue number B
128
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 82 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 128 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 75 and 128 (61 and 114 respectively in this structure).

Details

Redox score ?
69
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
5
% buried
42
Peptide accession
Q53H47
Residue number A
75
Residue number B
128
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 75 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 128 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 87 and 122 (73 and 108 respectively in this structure).

Details

Redox score ?
68
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
44
Peptide accession
Q53H47
Residue number A
87
Residue number B
122
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 87 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 122 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 87 and 124 (73 and 110 respectively in this structure).

Details

Redox score ?
68
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
38
Peptide accession
Q53H47
Residue number A
87
Residue number B
124
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 87 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 124 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 82 and 118 (68 and 104 respectively in this structure).

Details

Redox score ?
68
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
nan
Peptide accession
Q53H47
Residue number A
82
Residue number B
118
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 82 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 118 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 77 and 124 (63 and 110 respectively in this structure).

Details

Redox score ?
67
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
52
Minimum pKa ?
8
% buried
23
Peptide accession
Q53H47
Residue number A
77
Residue number B
124
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 77 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 124 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 87 and 128 (73 and 114 respectively in this structure).

Details

Redox score ?
66
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
46
Peptide accession
Q53H47
Residue number A
87
Residue number B
128
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 87 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 128 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 82 and 122 (68 and 108 respectively in this structure).

Details

Redox score ?
65
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
41
Peptide accession
Q53H47
Residue number A
82
Residue number B
122
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 82 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 122 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 89 and 124 (75 and 110 respectively in this structure).

Details

Redox score ?
62
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
8
% buried
46
Peptide accession
Q53H47
Residue number A
89
Residue number B
124
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 89 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 124 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 118 and 128 (104 and 114 respectively in this structure).

Details

Redox score ?
61
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
15
% buried
nan
Peptide accession
Q53H47
Residue number A
118
Residue number B
128
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 118 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 128 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 77 and 122 (63 and 108 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
28
Peptide accession
Q53H47
Residue number A
77
Residue number B
122
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 77 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 122 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 77 and 118 (63 and 104 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
nan
Peptide accession
Q53H47
Residue number A
77
Residue number B
118
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 77 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 118 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 77 and 89 (63 and 75 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
32
Peptide accession
Q53H47
Residue number A
77
Residue number B
89
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 77 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 89 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 122 and 128 (108 and 114 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
49
Peptide accession
Q53H47
Residue number A
122
Residue number B
128
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 122 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 128 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 82 and 89 (68 and 75 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
44
Peptide accession
Q53H47
Residue number A
82
Residue number B
89
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 82 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 89 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETMAR between cysteines 77 and 128 (63 and 114 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
3bo5
Structure name
crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
Structure deposition date
2007-12-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
30
Peptide accession
Q53H47
Residue number A
77
Residue number B
128
Peptide name
Histone-lysine N-methyltransferase SETMAR

Ligandability

Cysteine 77 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 128 of Histone-lysine N-methyltransferase SETMAR

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

If this tool was useful for finding a disulphide, please cite: