ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

COP9 signalosome complex subunit 1

Intramolecular
Cysteine 192 and cysteine 202
Cysteine 251 and cysteine 278
Cysteine 251 and cysteine 269
Cysteine 175 and cysteine 184
Cysteine 269 and cysteine 296
A redox-regulated disulphide may form within COP9 signalosome complex subunit 1 between cysteines 192 and 202 (228 and 238 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4d10
Structure name
crystal structure of the cop9 signalosome
Structure deposition date
2014-04-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
40
Peptide accession
Q13098
Residue number A
192
Residue number B
202
Peptide name
COP9 signalosome complex subunit 1

Ligandability

Cysteine 192 of COP9 signalosome complex subunit 1

Cysteine 202 of COP9 signalosome complex subunit 1

A redox-regulated disulphide may form within COP9 signalosome complex subunit 1 between cysteines 251 and 278 (287 and 314 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
6r7n
Structure name
structural basis of cullin-2 ring e3 ligase regulation by the cop9 signalosome
Structure deposition date
2019-03-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
72
Peptide accession
Q13098
Residue number A
251
Residue number B
278
Peptide name
COP9 signalosome complex subunit 1

Ligandability

Cysteine 251 of COP9 signalosome complex subunit 1

Cysteine 278 of COP9 signalosome complex subunit 1

A redox-regulated disulphide may form within COP9 signalosome complex subunit 1 between cysteines 251 and 269 (287 and 305 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4d10
Structure name
crystal structure of the cop9 signalosome
Structure deposition date
2014-04-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
10
% buried
76
Peptide accession
Q13098
Residue number A
251
Residue number B
269
Peptide name
COP9 signalosome complex subunit 1

Ligandability

Cysteine 251 of COP9 signalosome complex subunit 1

Cysteine 269 of COP9 signalosome complex subunit 1

A redox-regulated disulphide may form within COP9 signalosome complex subunit 1 between cysteines 175 and 184. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6r7f
Structure name
structural basis of cullin-2 ring e3 ligase regulation by the cop9 signalosome
Structure deposition date
2019-03-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
56
Peptide accession
Q13098
Residue number A
175
Residue number B
184
Peptide name
COP9 signalosome complex subunit 1

Ligandability

Cysteine 175 of COP9 signalosome complex subunit 1

Cysteine 184 of COP9 signalosome complex subunit 1

A redox-regulated disulphide may form within COP9 signalosome complex subunit 1 between cysteines 269 and 296 (305 and 332 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6r6h
Structure name
structural basis of cullin-2 ring e3 ligase regulation by the cop9 signalosome
Structure deposition date
2019-03-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
10
% buried
75
Peptide accession
Q13098
Residue number A
269
Residue number B
296
Peptide name
COP9 signalosome complex subunit 1

Ligandability

Cysteine 269 of COP9 signalosome complex subunit 1

Cysteine 296 of COP9 signalosome complex subunit 1

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