ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Cullin-1

Intramolecular
Cysteine 53 and cysteine 137
Cysteine 426 and cysteine 496
A redox-regulated disulphide may form within Cullin-1 between cysteines 53 and 137. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
1ldj
Structure name
structure of the cul1-rbx1-skp1-f boxskp2 scf ubiquitin ligase complex
Structure deposition date
2002-04-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
75
Peptide accession
Q13616
Residue number A
53
Residue number B
137
Peptide name
Cullin-1

Ligandability

Cysteine 53 of Cullin-1

Cysteine 137 of Cullin-1

A redox-regulated disulphide may form within Cullin-1 between cysteines 426 and 496 (425 and 495 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
1u6g
Structure name
crystal structure of the cand1-cul1-roc1 complex
Structure deposition date
2004-07-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
100
Peptide accession
Q13616
Residue number A
426
Residue number B
496
Peptide name
Cullin-1

Ligandability

Cysteine 426 of Cullin-1

Cysteine 496 of Cullin-1

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