ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase TRIM37

Intermolecular
Cysteine 66 and cysteine 66
Intramolecular
Cysteine 15 and cysteine 18
Cysteine 51 and cysteine 54
Cysteine 31 and cysteine 51
Cysteine 28 and cysteine 51
Cysteine 15 and cysteine 36
Cysteine 18 and cysteine 36
Cysteine 18 and cysteine 39
Cysteine 28 and cysteine 54
Cysteine 36 and cysteine 39
More...
Cysteine 31 and cysteine 54
Cysteine 35 and cysteine 51
Cysteine 28 and cysteine 31
Cysteine 35 and cysteine 36
Cysteine 15 and cysteine 35
Cysteine 15 and cysteine 39
Cysteine 35 and cysteine 39
Cysteine 31 and cysteine 35
Cysteine 28 and cysteine 35
Cysteine 18 and cysteine 35
A redox-regulated disulphide may form between two units of E3 ubiquitin-protein ligase TRIM37 at cysteines 66 and 66. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
13
% buried
97
Peptide A name
E3 ubiquitin-protein ligase TRIM37
Peptide B name
E3 ubiquitin-protein ligase TRIM37
Peptide A accession
O94972
Peptide B accession
O94972
Peptide A residue number
66
Peptide B residue number
66

Ligandability

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 15 and 18.

Details

Redox score ?
96
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
3
% buried
26
Peptide accession
O94972
Residue number A
15
Residue number B
18
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 15 of E3 ubiquitin-protein ligase TRIM37

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 18 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 51 and 54.

Details

Redox score ?
94
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
0
% buried
28
Peptide accession
O94972
Residue number A
51
Residue number B
54
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 51 of E3 ubiquitin-protein ligase TRIM37

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 54 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 31 and 51.

Details

Redox score ?
91
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
0
% buried
44
Peptide accession
O94972
Residue number A
31
Residue number B
51
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 31 of E3 ubiquitin-protein ligase TRIM37

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 51 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 28 and 51.

Details

Redox score ?
90
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
1
% buried
56
Peptide accession
O94972
Residue number A
28
Residue number B
51
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 28 of E3 ubiquitin-protein ligase TRIM37

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 51 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 15 and 36.

Details

Redox score ?
88
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
3
% buried
42
Peptide accession
O94972
Residue number A
15
Residue number B
36
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 15 of E3 ubiquitin-protein ligase TRIM37

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 36 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 18 and 36.

Details

Redox score ?
84
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
6
% buried
48
Peptide accession
O94972
Residue number A
18
Residue number B
36
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 18 of E3 ubiquitin-protein ligase TRIM37

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 36 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 18 and 39.

Details

Redox score ?
82
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
10
Peptide accession
O94972
Residue number A
18
Residue number B
39
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 18 of E3 ubiquitin-protein ligase TRIM37

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 39 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 28 and 54.

Details

Redox score ?
78
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
34
Peptide accession
O94972
Residue number A
28
Residue number B
54
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 28 of E3 ubiquitin-protein ligase TRIM37

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 54 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 36 and 39.

Details

Redox score ?
78
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
48
Peptide accession
O94972
Residue number A
36
Residue number B
39
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 36 of E3 ubiquitin-protein ligase TRIM37

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 39 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 31 and 54.

Details

Redox score ?
76
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
32
Peptide accession
O94972
Residue number A
31
Residue number B
54
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 31 of E3 ubiquitin-protein ligase TRIM37

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 54 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 35 and 51.

Details

Redox score ?
68
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
73
Minimum pKa ?
3
% buried
60
Peptide accession
O94972
Residue number A
35
Residue number B
51
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 35 of E3 ubiquitin-protein ligase TRIM37

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 51 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 28 and 31.

Details

Redox score ?
67
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
54
Peptide accession
O94972
Residue number A
28
Residue number B
31
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 28 of E3 ubiquitin-protein ligase TRIM37

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 31 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 35 and 36.

Details

Redox score ?
64
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
69
Minimum pKa ?
6
% buried
64
Peptide accession
O94972
Residue number A
35
Residue number B
36
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 35 of E3 ubiquitin-protein ligase TRIM37

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 36 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 15 and 35. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
16
% buried
nan
Peptide accession
O94972
Residue number A
15
Residue number B
35
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 15 of E3 ubiquitin-protein ligase TRIM37

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 35 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 15 and 39. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
18
% buried
nan
Peptide accession
O94972
Residue number A
15
Residue number B
39
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 15 of E3 ubiquitin-protein ligase TRIM37

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 39 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 35 and 39. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
17
% buried
63
Peptide accession
O94972
Residue number A
35
Residue number B
39
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 35 of E3 ubiquitin-protein ligase TRIM37

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 39 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 31 and 35. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
57
Peptide accession
O94972
Residue number A
31
Residue number B
35
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 31 of E3 ubiquitin-protein ligase TRIM37

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 35 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 28 and 35. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
10
% buried
64
Peptide accession
O94972
Residue number A
28
Residue number B
35
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 28 of E3 ubiquitin-protein ligase TRIM37

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 35 of E3 ubiquitin-protein ligase TRIM37

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 E3 ubiquitin-protein ligase TRIM37 between cysteines 18 and 35. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3lrq
Structure name
crystal structure of the u-box domain of human ubiquitin-protein ligase (e3), northeast structural genomics consortium target hr4604d
Structure deposition date
2010-02-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
17
% buried
64
Peptide accession
O94972
Residue number A
18
Residue number B
35
Peptide name
E3 ubiquitin-protein ligase TRIM37

Ligandability

Cysteine 18 of E3 ubiquitin-protein ligase TRIM37

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 35 of E3 ubiquitin-protein ligase TRIM37

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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