ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

AP-2 complex subunit alpha

Intramolecular
Cysteine 492 and cysteine 533
Cysteine 134 and cysteine 171
A redox-regulated disulphide may form within AP-2 complex subunit alpha between cysteines 492 and 533. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2xa7
Structure name
ap2 clathrin adaptor core in active complex with cargo peptides
Structure deposition date
2010-03-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
69
Peptide accession
Q66HM2
Residue number A
492
Residue number B
533
Peptide name
AP-2 complex subunit alpha

Ligandability

Cysteine 492 of AP-2 complex subunit alpha

Cysteine 533 of AP-2 complex subunit alpha

A redox-regulated disulphide may form within AP-2 complex subunit alpha between cysteines 134 and 171. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
6uri
Structure name
hiv-1 nef in complex with the cd4 cytoplasmic domain and the ap2 clathrin adaptor complex
Structure deposition date
2019-10-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
100
Minimum pKa ?
12
% buried
100
Peptide accession
Q66HM2
Residue number A
134
Residue number B
171
Peptide name
AP-2 complex subunit alpha

Ligandability

Cysteine 134 of AP-2 complex subunit alpha

Cysteine 171 of AP-2 complex subunit alpha

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