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a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase ARIH2

Intramolecular
Cysteine 139 and cysteine 142
Cysteine 139 and cysteine 161
Cysteine 315 and cysteine 318
Cysteine 257 and cysteine 270
Cysteine 233 and cysteine 249
Cysteine 257 and cysteine 260
Cysteine 300 and cysteine 315
Cysteine 297 and cysteine 318
Cysteine 139 and cysteine 164
Cysteine 233 and cysteine 252
More...
Cysteine 142 and cysteine 161
Cysteine 297 and cysteine 300
Cysteine 297 and cysteine 315
Cysteine 249 and cysteine 252
Cysteine 156 and cysteine 188
Cysteine 228 and cysteine 249
Cysteine 142 and cysteine 164
Cysteine 300 and cysteine 318
Cysteine 156 and cysteine 183
Cysteine 183 and cysteine 188
Cysteine 228 and cysteine 252
Cysteine 326 and cysteine 340
Cysteine 323 and cysteine 340 L
Cysteine 228 and cysteine 233
Cysteine 161 and cysteine 164
Cysteine 260 and cysteine 270
Cysteine 63 and cysteine 249
Cysteine 323 and cysteine 326 L
Cysteine 63 and cysteine 233
Cysteine 63 and cysteine 252
Cysteine 63 and cysteine 228
Cysteine 310 and cysteine 323 L
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase ARIH2 between cysteines 139 and 142.

Details

Redox score ?
94
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
5
% buried
0
Peptide accession
O95376
Residue number A
139
Residue number B
142
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 139 of E3 ubiquitin-protein ligase ARIH2

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 142 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 139 and 161.

Details

Redox score ?
92
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
5
% buried
0
Peptide accession
O95376
Residue number A
139
Residue number B
161
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 139 of E3 ubiquitin-protein ligase ARIH2

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 161 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 315 and 318.

Details

Redox score ?
90
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
6
% buried
0
Peptide accession
O95376
Residue number A
315
Residue number B
318
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 315 of E3 ubiquitin-protein ligase ARIH2

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 318 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 257 and 270.

Details

Redox score ?
87
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
2
% buried
49
Peptide accession
O95376
Residue number A
257
Residue number B
270
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 257 of E3 ubiquitin-protein ligase ARIH2

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 270 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 233 and 249.

Details

Redox score ?
86
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
7
% buried
35
Peptide accession
O95376
Residue number A
233
Residue number B
249
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 233 of E3 ubiquitin-protein ligase ARIH2

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 249 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 257 and 260.

Details

Redox score ?
85
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
2
% buried
54
Peptide accession
O95376
Residue number A
257
Residue number B
260
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 257 of E3 ubiquitin-protein ligase ARIH2

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 260 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 300 and 315.

Details

Redox score ?
85
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
0
Peptide accession
O95376
Residue number A
300
Residue number B
315
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 300 of E3 ubiquitin-protein ligase ARIH2

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 315 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 297 and 318.

Details

Redox score ?
84
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
7
% buried
0
Peptide accession
O95376
Residue number A
297
Residue number B
318
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 297 of E3 ubiquitin-protein ligase ARIH2

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 318 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 139 and 164.

Details

Redox score ?
84
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
5
% buried
10
Peptide accession
O95376
Residue number A
139
Residue number B
164
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 139 of E3 ubiquitin-protein ligase ARIH2

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 164 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 233 and 252.

Details

Redox score ?
83
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
8
% buried
20
Peptide accession
O95376
Residue number A
233
Residue number B
252
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 233 of E3 ubiquitin-protein ligase ARIH2

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 252 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 142 and 161.

Details

Redox score ?
83
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
4
Peptide accession
O95376
Residue number A
142
Residue number B
161
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 142 of E3 ubiquitin-protein ligase ARIH2

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 161 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 297 and 300.

Details

Redox score ?
82
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
0
Peptide accession
O95376
Residue number A
297
Residue number B
300
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 297 of E3 ubiquitin-protein ligase ARIH2

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 300 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 297 and 315.

Details

Redox score ?
82
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
0
Peptide accession
O95376
Residue number A
297
Residue number B
315
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 297 of E3 ubiquitin-protein ligase ARIH2

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 315 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 249 and 252.

Details

Redox score ?
81
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
28
Peptide accession
O95376
Residue number A
249
Residue number B
252
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 249 of E3 ubiquitin-protein ligase ARIH2

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 252 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 156 and 188.

Details

Redox score ?
81
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
19
Peptide accession
O95376
Residue number A
156
Residue number B
188
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 156 of E3 ubiquitin-protein ligase ARIH2

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 188 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 228 and 249.

Details

Redox score ?
81
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
7
% buried
42
Peptide accession
O95376
Residue number A
228
Residue number B
249
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 228 of E3 ubiquitin-protein ligase ARIH2

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 249 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 142 and 164.

Details

Redox score ?
80
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
4
Peptide accession
O95376
Residue number A
142
Residue number B
164
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 142 of E3 ubiquitin-protein ligase ARIH2

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 164 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 300 and 318.

Details

Redox score ?
80
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
35
Minimum pKa ?
9
% buried
0
Peptide accession
O95376
Residue number A
300
Residue number B
318
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 300 of E3 ubiquitin-protein ligase ARIH2

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 318 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 156 and 183.

Details

Redox score ?
80
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
28
Peptide accession
O95376
Residue number A
156
Residue number B
183
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 156 of E3 ubiquitin-protein ligase ARIH2

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 183 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 183 and 188.

Details

Redox score ?
79
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
22
Peptide accession
O95376
Residue number A
183
Residue number B
188
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 183 of E3 ubiquitin-protein ligase ARIH2

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 188 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 228 and 252.

Details

Redox score ?
78
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
27
Peptide accession
O95376
Residue number A
228
Residue number B
252
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 228 of E3 ubiquitin-protein ligase ARIH2

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 252 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 326 and 340.

Details

Redox score ?
77
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
6
% buried
71
Peptide accession
O95376
Residue number A
326
Residue number B
340
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 326 of E3 ubiquitin-protein ligase ARIH2

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 340 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 323 and 340.

Details

Redox score ?
77
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
6
% buried
nan
Peptide accession
O95376
Residue number A
323
Residue number B
340
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 323 of E3 ubiquitin-protein ligase ARIH2

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 340 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 228 and 233.

Details

Redox score ?
77
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
34
Peptide accession
O95376
Residue number A
228
Residue number B
233
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 228 of E3 ubiquitin-protein ligase ARIH2

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 E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 161 and 164.

Details

Redox score ?
76
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
8
Peptide accession
O95376
Residue number A
161
Residue number B
164
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 161 of E3 ubiquitin-protein ligase ARIH2

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 164 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 260 and 270.

Details

Redox score ?
72
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
41
Peptide accession
O95376
Residue number A
260
Residue number B
270
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 260 of E3 ubiquitin-protein ligase ARIH2

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 270 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 63 and 249.

Details

Redox score ?
70
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
7
% buried
64
Peptide accession
O95376
Residue number A
63
Residue number B
249
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 63 of E3 ubiquitin-protein ligase ARIH2

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 249 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 323 and 326. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
18
% buried
nan
Peptide accession
O95376
Residue number A
323
Residue number B
326
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 323 of E3 ubiquitin-protein ligase ARIH2

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 326 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 63 and 233. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
51
Peptide accession
O95376
Residue number A
63
Residue number B
233
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 63 of E3 ubiquitin-protein ligase ARIH2

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 E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 63 and 252. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
47
Peptide accession
O95376
Residue number A
63
Residue number B
252
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 63 of E3 ubiquitin-protein ligase ARIH2

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 252 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 63 and 228. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
58
Peptide accession
O95376
Residue number A
63
Residue number B
228
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 63 of E3 ubiquitin-protein ligase ARIH2

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 228 of E3 ubiquitin-protein ligase ARIH2

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 ARIH2 between cysteines 310 and 323. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
7od1
Structure name
crystal structure of rbr ubiquitin ligase arih2
Structure deposition date
2021-04-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
96
Peptide accession
O95376
Residue number A
310
Residue number B
323
Peptide name
E3 ubiquitin-protein ligase ARIH2

Ligandability

Cysteine 310 of E3 ubiquitin-protein ligase ARIH2

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 323 of E3 ubiquitin-protein ligase ARIH2

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.

Ligandable in the dataset of Kuljanin et al.

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