ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Cullin-3

Intramolecular
Cysteine 187 and cysteine 251
Cysteine 314 and cysteine 316
A redox-regulated disulphide may form within Cullin-3 between cysteines 187 and 251. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4eoz
Structure name
crystal structure of the spop btb domain complexed with the cul3 n- terminal domain
Structure deposition date
2012-04-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
76
Peptide accession
Q13618
Residue number A
187
Residue number B
251
Peptide name
Cullin-3

Ligandability

Cysteine 187 of Cullin-3

Cysteine 251 of Cullin-3

A redox-regulated disulphide may form within Cullin-3 between cysteines 314 and 316. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
5nlb
Structure name
crystal structure of human cul3 n-terminal domain bound to keap1 btb and 3-box
Structure deposition date
2017-04-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
59
Peptide accession
Q13618
Residue number A
314
Residue number B
316
Peptide name
Cullin-3

Ligandability

Cysteine 314 of Cullin-3

Cysteine 316 of Cullin-3

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