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Histone-lysine N-methyltransferase SUV39H2

Intramolecular
Cysteine 235 and cysteine 239
Cysteine 191 and cysteine 193
Cysteine 191 and cysteine 196
Cysteine 400 and cysteine 405
Cysteine 398 and cysteine 405
Cysteine 333 and cysteine 405
Cysteine 191 and cysteine 229
Cysteine 398 and cysteine 400
Cysteine 333 and cysteine 400
Cysteine 229 and cysteine 233
More...
Cysteine 191 and cysteine 233
Cysteine 193 and cysteine 196
Cysteine 201 and cysteine 239
Cysteine 202 and cysteine 233
Cysteine 196 and cysteine 235
Cysteine 333 and cysteine 398
Cysteine 196 and cysteine 201
Cysteine 196 and cysteine 239
Cysteine 191 and cysteine 239
Cysteine 193 and cysteine 201
Cysteine 191 and cysteine 201
Cysteine 229 and cysteine 235
Cysteine 201 and cysteine 229
Cysteine 233 and cysteine 235
Cysteine 191 and cysteine 235
Cysteine 229 and cysteine 239
Cysteine 196 and cysteine 229
Cysteine 193 and cysteine 239
Cysteine 191 and cysteine 202
Cysteine 202 and cysteine 229
Cysteine 201 and cysteine 235
Cysteine 201 and cysteine 202
Cysteine 196 and cysteine 233
Cysteine 201 and cysteine 233
Cysteine 193 and cysteine 235
Cysteine 202 and cysteine 235
Cysteine 193 and cysteine 229
Cysteine 193 and cysteine 233
Cysteine 193 and cysteine 202
Cysteine 233 and cysteine 239
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SUV39H2 between cysteines 235 and 239 (124 and 128 respectively in this structure).

Details

Redox score ?
92
PDB code
2r3a
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Structure deposition date
2007-08-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
3
% buried
34
Peptide accession
Q9H5I1
Residue number A
235
Residue number B
239
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 235 of Histone-lysine N-methyltransferase SUV39H2

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 239 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 191 and 193 (80 and 82 respectively in this structure).

Details

Redox score ?
88
PDB code
2r3a
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Structure deposition date
2007-08-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
5
% buried
17
Peptide accession
Q9H5I1
Residue number A
191
Residue number B
193
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 191 of Histone-lysine N-methyltransferase SUV39H2

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 193 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 191 and 196 (80 and 85 respectively in this structure).

Details

Redox score ?
88
PDB code
2r3a
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Structure deposition date
2007-08-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
5
% buried
28
Peptide accession
Q9H5I1
Residue number A
191
Residue number B
196
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 191 of Histone-lysine N-methyltransferase SUV39H2

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 196 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 400 and 405 (289 and 294 respectively in this structure).

Details

Redox score ?
87
PDB code
2r3a
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Structure deposition date
2007-08-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
12
Peptide accession
Q9H5I1
Residue number A
400
Residue number B
405
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 400 of Histone-lysine N-methyltransferase SUV39H2

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 405 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 398 and 405.

Details

Redox score ?
83
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
38
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
398
Residue number B
405
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 398 of Histone-lysine N-methyltransferase SUV39H2

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 405 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 333 and 405 (222 and 294 respectively in this structure).

Details

Redox score ?
83
PDB code
2r3a
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Structure deposition date
2007-08-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
6
Peptide accession
Q9H5I1
Residue number A
333
Residue number B
405
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 333 of Histone-lysine N-methyltransferase SUV39H2

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 405 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 191 and 229 (80 and 118 respectively in this structure).

Details

Redox score ?
82
PDB code
2r3a
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Structure deposition date
2007-08-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
5
% buried
40
Peptide accession
Q9H5I1
Residue number A
191
Residue number B
229
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 191 of Histone-lysine N-methyltransferase SUV39H2

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 229 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 398 and 400.

Details

Redox score ?
82
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
398
Residue number B
400
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 398 of Histone-lysine N-methyltransferase SUV39H2

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 400 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 333 and 400.

Details

Redox score ?
80
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
333
Residue number B
400
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 333 of Histone-lysine N-methyltransferase SUV39H2

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 400 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 229 and 233 (118 and 122 respectively in this structure).

Details

Redox score ?
80
PDB code
2r3a
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Structure deposition date
2007-08-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
44
Peptide accession
Q9H5I1
Residue number A
229
Residue number B
233
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 229 of Histone-lysine N-methyltransferase SUV39H2

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 233 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 191 and 233.

Details

Redox score ?
79
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
191
Residue number B
233
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 191 of Histone-lysine N-methyltransferase SUV39H2

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 233 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 193 and 196.

Details

Redox score ?
78
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
193
Residue number B
196
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 193 of Histone-lysine N-methyltransferase SUV39H2

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 196 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 201 and 239 (90 and 128 respectively in this structure).

Details

Redox score ?
78
PDB code
2r3a
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Structure deposition date
2007-08-29
Thiol separation (Å)
6
Half-sphere exposure sum ?
66
Minimum pKa ?
3
% buried
nan
Peptide accession
Q9H5I1
Residue number A
201
Residue number B
239
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 201 of Histone-lysine N-methyltransferase SUV39H2

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 239 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 202 and 233.

Details

Redox score ?
78
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
202
Residue number B
233
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 202 of Histone-lysine N-methyltransferase SUV39H2

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 233 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 196 and 235.

Details

Redox score ?
78
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
196
Residue number B
235
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 196 of Histone-lysine N-methyltransferase SUV39H2

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 235 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 333 and 398 (222 and 287 respectively in this structure).

Details

Redox score ?
77
PDB code
2r3a
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Structure deposition date
2007-08-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
21
Peptide accession
Q9H5I1
Residue number A
333
Residue number B
398
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 333 of Histone-lysine N-methyltransferase SUV39H2

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 398 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 196 and 201.

Details

Redox score ?
77
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
196
Residue number B
201
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 196 of Histone-lysine N-methyltransferase SUV39H2

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 201 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 196 and 239.

Details

Redox score ?
77
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
196
Residue number B
239
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 196 of Histone-lysine N-methyltransferase SUV39H2

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 239 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 191 and 239 (80 and 128 respectively in this structure).

Details

Redox score ?
76
PDB code
2r3a
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Structure deposition date
2007-08-29
Thiol separation (Å)
6
Half-sphere exposure sum ?
63
Minimum pKa ?
3
% buried
34
Peptide accession
Q9H5I1
Residue number A
191
Residue number B
239
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 191 of Histone-lysine N-methyltransferase SUV39H2

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 239 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 193 and 201 (82 and 90 respectively in this structure).

Details

Redox score ?
75
PDB code
2r3a
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Structure deposition date
2007-08-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9H5I1
Residue number A
193
Residue number B
201
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 193 of Histone-lysine N-methyltransferase SUV39H2

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 201 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 191 and 201.

Details

Redox score ?
75
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
191
Residue number B
201
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 191 of Histone-lysine N-methyltransferase SUV39H2

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 201 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 229 and 235.

Details

Redox score ?
74
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
229
Residue number B
235
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 229 of Histone-lysine N-methyltransferase SUV39H2

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 235 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 201 and 229.

Details

Redox score ?
74
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
201
Residue number B
229
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 201 of Histone-lysine N-methyltransferase SUV39H2

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 229 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 233 and 235.

Details

Redox score ?
73
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
233
Residue number B
235
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 233 of Histone-lysine N-methyltransferase SUV39H2

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 235 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 191 and 235.

Details

Redox score ?
73
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
191
Residue number B
235
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 191 of Histone-lysine N-methyltransferase SUV39H2

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 235 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 229 and 239.

Details

Redox score ?
72
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
229
Residue number B
239
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 229 of Histone-lysine N-methyltransferase SUV39H2

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 239 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 196 and 229.

Details

Redox score ?
72
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
196
Residue number B
229
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 196 of Histone-lysine N-methyltransferase SUV39H2

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 229 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 193 and 239 (82 and 128 respectively in this structure).

Details

Redox score ?
71
PDB code
2r3a
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Structure deposition date
2007-08-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
55
Minimum pKa ?
3
% buried
26
Peptide accession
Q9H5I1
Residue number A
193
Residue number B
239
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 193 of Histone-lysine N-methyltransferase SUV39H2

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 239 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 191 and 202.

Details

Redox score ?
70
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
191
Residue number B
202
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 191 of Histone-lysine N-methyltransferase SUV39H2

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 202 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 202 and 229.

Details

Redox score ?
67
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
202
Residue number B
229
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 202 of Histone-lysine N-methyltransferase SUV39H2

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 229 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 201 and 235 (90 and 124 respectively in this structure).

Details

Redox score ?
64
PDB code
2r3a
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Structure deposition date
2007-08-29
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
nan
Peptide accession
Q9H5I1
Residue number A
201
Residue number B
235
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 201 of Histone-lysine N-methyltransferase SUV39H2

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 235 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 201 and 202 (90 and 91 respectively in this structure).

Details

Redox score ?
64
PDB code
2r3a
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Structure deposition date
2007-08-29
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
nan
Peptide accession
Q9H5I1
Residue number A
201
Residue number B
202
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 201 of Histone-lysine N-methyltransferase SUV39H2

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 202 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 196 and 233.

Details

Redox score ?
64
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
196
Residue number B
233
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 196 of Histone-lysine N-methyltransferase SUV39H2

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 233 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 201 and 233.

Details

Redox score ?
64
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
201
Residue number B
233
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 201 of Histone-lysine N-methyltransferase SUV39H2

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 233 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 193 and 235.

Details

Redox score ?
61
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
193
Residue number B
235
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 193 of Histone-lysine N-methyltransferase SUV39H2

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 235 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 202 and 235 (91 and 124 respectively in this structure).

Details

Redox score ?
60
PDB code
2r3a
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Structure deposition date
2007-08-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
8
% buried
35
Peptide accession
Q9H5I1
Residue number A
202
Residue number B
235
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 202 of Histone-lysine N-methyltransferase SUV39H2

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 235 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 193 and 229.

Details

Redox score ?
60
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
193
Residue number B
229
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 193 of Histone-lysine N-methyltransferase SUV39H2

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 229 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 193 and 233. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
193
Residue number B
233
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 193 of Histone-lysine N-methyltransferase SUV39H2

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 233 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 193 and 202 (82 and 91 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
2r3a
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Structure deposition date
2007-08-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
27
Peptide accession
Q9H5I1
Residue number A
193
Residue number B
202
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 193 of Histone-lysine N-methyltransferase SUV39H2

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 202 of Histone-lysine N-methyltransferase SUV39H2

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 SUV39H2 between cysteines 233 and 239. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
6p0r
Structure name
methyltransferase domain of human suppressor of variegation 3-9 homolog 2 (suv39h2) in complex with ots186935 inhibitor
Structure deposition date
2019-05-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H5I1
Residue number A
233
Residue number B
239
Peptide name
Histone-lysine N-methyltransferase SUV39H2

Ligandability

Cysteine 233 of Histone-lysine N-methyltransferase SUV39H2

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 239 of Histone-lysine N-methyltransferase SUV39H2

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.

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