ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

E3 ubiquitin-protein ligase RNF4

Intramolecular
Cysteine 158 and cysteine 180
Cysteine 139 and cysteine 166
Cysteine 136 and cysteine 166
Cysteine 177 and cysteine 180
Cysteine 139 and cysteine 163
Cysteine 158 and cysteine 177
Cysteine 136 and cysteine 163
Cysteine 132 and cysteine 173
Cysteine 136 and cysteine 139
Cysteine 163 and cysteine 166
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF4 between cysteines 158 and 180.

Details

Redox score ?
84
PDB code
3ng2
Structure name
crystal structure of the rnf4 ring domain dimer
Structure deposition date
2010-06-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
8
% buried
0
Peptide accession
O88846
Residue number A
158
Residue number B
180
Peptide name
E3 ubiquitin-protein ligase RNF4

Ligandability

Cysteine 158 of E3 ubiquitin-protein ligase RNF4

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 180 of E3 ubiquitin-protein ligase RNF4

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 RNF4 between cysteines 139 and 166.

Details

Redox score ?
82
PDB code
5ait
Structure name
a complex of of rnf4-ring domain, ubev2, ubc13-ub (isopeptide crosslink)
Structure deposition date
2015-02-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
4
% buried
68
Peptide accession
O88846
Residue number A
139
Residue number B
166
Peptide name
E3 ubiquitin-protein ligase RNF4

Ligandability

Cysteine 139 of E3 ubiquitin-protein ligase RNF4

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 166 of E3 ubiquitin-protein ligase RNF4

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 RNF4 between cysteines 136 and 166.

Details

Redox score ?
81
PDB code
3ng2
Structure name
crystal structure of the rnf4 ring domain dimer
Structure deposition date
2010-06-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
7
% buried
12
Peptide accession
O88846
Residue number A
136
Residue number B
166
Peptide name
E3 ubiquitin-protein ligase RNF4

Ligandability

Cysteine 136 of E3 ubiquitin-protein ligase RNF4

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 166 of E3 ubiquitin-protein ligase RNF4

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 RNF4 between cysteines 177 and 180 (242 and 245 respectively in this structure).

Details

Redox score ?
80
PDB code
5ait
Structure name
a complex of of rnf4-ring domain, ubev2, ubc13-ub (isopeptide crosslink)
Structure deposition date
2015-02-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
7
% buried
32
Peptide accession
O88846
Residue number A
177
Residue number B
180
Peptide name
E3 ubiquitin-protein ligase RNF4

Ligandability

Cysteine 177 of E3 ubiquitin-protein ligase RNF4

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 180 of E3 ubiquitin-protein ligase RNF4

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 RNF4 between cysteines 139 and 163 (204 and 228 respectively in this structure).

Details

Redox score ?
79
PDB code
5aiu
Structure name
a complex of rnf4-ring domain, ubc13-ub (isopeptide crosslink)
Structure deposition date
2015-02-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
5
% buried
60
Peptide accession
O88846
Residue number A
139
Residue number B
163
Peptide name
E3 ubiquitin-protein ligase RNF4

Ligandability

Cysteine 139 of E3 ubiquitin-protein ligase RNF4

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 163 of E3 ubiquitin-protein ligase RNF4

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 RNF4 between cysteines 158 and 177.

Details

Redox score ?
71
PDB code
5ait
Structure name
a complex of of rnf4-ring domain, ubev2, ubc13-ub (isopeptide crosslink)
Structure deposition date
2015-02-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
nan
Peptide accession
O88846
Residue number A
158
Residue number B
177
Peptide name
E3 ubiquitin-protein ligase RNF4

Ligandability

Cysteine 158 of E3 ubiquitin-protein ligase RNF4

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 177 of E3 ubiquitin-protein ligase RNF4

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 RNF4 between cysteines 136 and 163.

Details

Redox score ?
65
PDB code
5ait
Structure name
a complex of of rnf4-ring domain, ubev2, ubc13-ub (isopeptide crosslink)
Structure deposition date
2015-02-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
14
% buried
nan
Peptide accession
O88846
Residue number A
136
Residue number B
163
Peptide name
E3 ubiquitin-protein ligase RNF4

Ligandability

Cysteine 136 of E3 ubiquitin-protein ligase RNF4

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 163 of E3 ubiquitin-protein ligase RNF4

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 RNF4 between cysteines 132 and 173 (18 and 59 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
2ea6
Structure name
solution structure of the ring domain of the human ring finger protein 4
Structure deposition date
2007-01-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
6
% buried
10
Peptide accession
P78317
Residue number A
132
Residue number B
173
Peptide name
E3 ubiquitin-protein ligase RNF4

Ligandability

Cysteine 132 of E3 ubiquitin-protein ligase RNF4

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 173 of E3 ubiquitin-protein ligase RNF4

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 RNF4 between cysteines 136 and 139 (201 and 204 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
5ait
Structure name
a complex of of rnf4-ring domain, ubev2, ubc13-ub (isopeptide crosslink)
Structure deposition date
2015-02-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
70
Minimum pKa ?
23
% buried
nan
Peptide accession
O88846
Residue number A
136
Residue number B
139
Peptide name
E3 ubiquitin-protein ligase RNF4

Ligandability

Cysteine 136 of E3 ubiquitin-protein ligase RNF4

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 139 of E3 ubiquitin-protein ligase RNF4

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 RNF4 between cysteines 163 and 166. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
5ait
Structure name
a complex of of rnf4-ring domain, ubev2, ubc13-ub (isopeptide crosslink)
Structure deposition date
2015-02-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
71
Minimum pKa ?
23
% buried
nan
Peptide accession
O88846
Residue number A
163
Residue number B
166
Peptide name
E3 ubiquitin-protein ligase RNF4

Ligandability

Cysteine 163 of E3 ubiquitin-protein ligase RNF4

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 166 of E3 ubiquitin-protein ligase RNF4

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: