Cullin-2
Intramolecular
Cysteine 250 and cysteine 266
Cysteine 232 and cysteine 282
Cysteine 385 and cysteine 465
5n4w A 250 A 266
A redox-regulated disulphide may form within Cullin-2 between cysteines 250 and 266. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
5n4w
Structure name
crystal structure of the cul2-rbx1-elobc-vhl ubiquitin ligase complex
Structure deposition date
2017-02-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
66
Minimum pKa ?
12
% buried
78
Peptide accession
Q13617
Residue number A
250
Residue number B
266
Peptide name
Cullin-2
Ligandability
Cysteine 250 of Cullin-2
Cysteine 266 of Cullin-2
5n4w A 232 A 282
A redox-regulated disulphide may form within Cullin-2 between cysteines 232 and 282. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
5n4w
Structure name
crystal structure of the cul2-rbx1-elobc-vhl ubiquitin ligase complex
Structure deposition date
2017-02-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
55
Peptide accession
Q13617
Residue number A
232
Residue number B
282
Peptide name
Cullin-2
Ligandability
Cysteine 232 of Cullin-2
Cysteine 282 of Cullin-2
6r7i O 385 O 465
A redox-regulated disulphide may form within Cullin-2 between cysteines 385 and 465. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
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 ?
63
Minimum pKa ?
11
% buried
76
Peptide accession
Q13617
Residue number A
385
Residue number B
465
Peptide name
Cullin-2
Ligandability
Cysteine 385 of Cullin-2
Cysteine 465 of Cullin-2
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