COP9 signalosome complex subunit 6
Intermolecular
Cysteine 264 and cysteine 181 of COP9 signalosome complex subunit 7b
Cysteine 264 and cysteine 178 of COP9 signalosome complex subunit 7b
Cysteine 266 and cysteine 157 of COP9 signalosome complex subunit 7b
Cysteine 383 of COP9 signalosome complex subunit 3 and cysteine 299 L
Cysteine 378 of COP9 signalosome complex subunit 4 and cysteine 266
Cysteine 308 of COP9 signalosome complex subunit 5 and cysteine 299 L
Intramolecular
Cysteine 264 and cysteine 266
6r7i F 264 G 181
A redox-regulated disulphide may form between cysteine 264 of COP9 signalosome complex subunit 6 and cysteine 181 of COP9 signalosome complex subunit 7b. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
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)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
51
Peptide A name
COP9 signalosome complex subunit 6
Peptide B name
COP9 signalosome complex subunit 7b
Peptide A accession
Q7L5N1
Peptide B accession
Q9H9Q2
Peptide A residue number
264
Peptide B residue number
181
Ligandability
Cysteine 264 of COP9 signalosome complex subunit 6
Cysteine 181 of COP9 signalosome complex subunit 7b
6r6h F 264 G 178
A redox-regulated disulphide may form between cysteine 264 of COP9 signalosome complex subunit 6 and cysteine 178 of COP9 signalosome complex subunit 7b. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
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 ?
78
Minimum pKa ?
8
% buried
96
Peptide A name
COP9 signalosome complex subunit 6
Peptide B name
COP9 signalosome complex subunit 7b
Peptide A accession
Q7L5N1
Peptide B accession
Q9H9Q2
Peptide A residue number
264
Peptide B residue number
178
Ligandability
Cysteine 264 of COP9 signalosome complex subunit 6
Cysteine 178 of COP9 signalosome complex subunit 7b
6r7i F 266 G 157
A redox-regulated disulphide may form between cysteine 266 of COP9 signalosome complex subunit 6 and cysteine 157 of COP9 signalosome complex subunit 7b. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
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)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
11
% buried
98
Peptide A name
COP9 signalosome complex subunit 6
Peptide B name
COP9 signalosome complex subunit 7b
Peptide A accession
Q7L5N1
Peptide B accession
Q9H9Q2
Peptide A residue number
266
Peptide B residue number
157
Ligandability
Cysteine 266 of COP9 signalosome complex subunit 6
Cysteine 157 of COP9 signalosome complex subunit 7b
6r6h C 383 F 299
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
Cysteine 299 of COP9 signalosome complex subunit 6
6r7h D 378 F 266
A redox-regulated disulphide may form between cysteine 378 of COP9 signalosome complex subunit 4 and cysteine 266 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 ?
29
PDB code
6r7h
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 ?
70
Minimum pKa ?
12
% buried
99
Peptide A name
COP9 signalosome complex subunit 4
Peptide B name
COP9 signalosome complex subunit 6
Peptide A accession
Q9BT78
Peptide B accession
Q7L5N1
Peptide A residue number
378
Peptide B residue number
266
Ligandability
Cysteine 378 of COP9 signalosome complex subunit 4
Cysteine 266 of COP9 signalosome complex subunit 6
6r7i E 308 F 299
A redox-regulated disulphide may form between cysteine 308 of COP9 signalosome complex subunit 5 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 ?
28
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)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
98
Peptide A name
COP9 signalosome complex subunit 5
Peptide B name
COP9 signalosome complex subunit 6
Peptide A accession
Q92905
Peptide B accession
Q7L5N1
Peptide A residue number
308
Peptide B residue number
299
Ligandability
Cysteine 308 of COP9 signalosome complex subunit 5
Cysteine 299 of COP9 signalosome complex subunit 6
4d10 N 264 N 266
A redox-regulated disulphide may form within COP9 signalosome complex subunit 6 between cysteines 264 and 266. 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 ?
87
Minimum pKa ?
10
% buried
98
Peptide accession
Q7L5N1
Residue number A
264
Residue number B
266
Peptide name
COP9 signalosome complex subunit 6
Ligandability
Cysteine 264 of COP9 signalosome complex subunit 6
Cysteine 266 of COP9 signalosome complex subunit 6
If this tool was useful for finding a disulphide, please cite: