ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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COP9 signalosome complex subunit 3

Intermolecular
Cysteine 154 and cysteine 20 of COP9 signalosome complex subunit 8
Cysteine 383 and cysteine 299 of COP9 signalosome complex subunit 6 L
Intramolecular
Cysteine 146 and cysteine 149
Cysteine 149 and cysteine 154
Cysteine 25 and cysteine 88
Cysteine 146 and cysteine 183
A redox-regulated disulphide may form between cysteine 154 of COP9 signalosome complex subunit 3 and cysteine 20 of COP9 signalosome complex subunit 8. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
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)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
82
Peptide A name
COP9 signalosome complex subunit 3
Peptide B name
COP9 signalosome complex subunit 8
Peptide A accession
Q9UNS2
Peptide B accession
Q99627
Peptide A residue number
154
Peptide B residue number
20

Ligandability

Cysteine 154 of COP9 signalosome complex subunit 3

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 20 of COP9 signalosome complex subunit 8

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 between cysteine 383 of COP9 signalosome complex subunit 3 and cysteine 299 of COP9 signalosome complex subunit 6. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
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)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
11
% buried
100
Peptide A name
COP9 signalosome complex subunit 3
Peptide B name
COP9 signalosome complex subunit 6
Peptide A accession
Q9UNS2
Peptide B accession
Q7L5N1
Peptide A residue number
383
Peptide B residue number
299

Ligandability

Cysteine 383 of COP9 signalosome complex subunit 3

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 299 of COP9 signalosome complex subunit 6

Not ligandable in the dataset of Yang et al.

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 COP9 signalosome complex subunit 3 between cysteines 146 and 149. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
4d10
Structure name
crystal structure of the cop9 signalosome
Structure deposition date
2014-04-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
84
Minimum pKa ?
13
% buried
100
Peptide accession
Q9UNS2
Residue number A
146
Residue number B
149
Peptide name
COP9 signalosome complex subunit 3

Ligandability

Cysteine 146 of COP9 signalosome complex subunit 3

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 149 of COP9 signalosome complex subunit 3

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 COP9 signalosome complex subunit 3 between cysteines 149 and 154. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4d18
Structure name
crystal structure of the cop9 signalosome
Structure deposition date
2014-05-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
100
Peptide accession
Q9UNS2
Residue number A
149
Residue number B
154
Peptide name
COP9 signalosome complex subunit 3

Ligandability

Cysteine 149 of COP9 signalosome complex subunit 3

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 154 of COP9 signalosome complex subunit 3

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 COP9 signalosome complex subunit 3 between cysteines 25 and 88. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6r7i
Structure name
structural basis of cullin-2 ring e3 ligase regulation by the cop9 signalosome
Structure deposition date
2019-03-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
76
Peptide accession
Q9UNS2
Residue number A
25
Residue number B
88
Peptide name
COP9 signalosome complex subunit 3

Ligandability

Cysteine 25 of COP9 signalosome complex subunit 3

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 88 of COP9 signalosome complex subunit 3

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 COP9 signalosome complex subunit 3 between cysteines 146 and 183. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
4d10
Structure name
crystal structure of the cop9 signalosome
Structure deposition date
2014-04-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
86
Peptide accession
Q9UNS2
Residue number A
146
Residue number B
183
Peptide name
COP9 signalosome complex subunit 3

Ligandability

Cysteine 146 of COP9 signalosome complex subunit 3

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 COP9 signalosome complex subunit 3

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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