ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Importin subunit alpha-3

Intermolecular
Cysteine 248 and cysteine 248
Intramolecular
Cysteine 417 and cysteine 456
A redox-regulated disulphide may form between two units of Importin subunit alpha-3 at cysteines 248 and 248. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6wx8
Structure name
sox2 bound to importin-alpha 3
Structure deposition date
2020-05-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
94
Peptide A name
Importin subunit alpha-3
Peptide B name
Importin subunit alpha-3
Peptide A accession
O00629
Peptide B accession
O00629
Peptide A residue number
248
Peptide B residue number
248

Ligandability

A redox-regulated disulphide may form within Importin subunit alpha-3 between cysteines 417 and 456.

Details

Redox score ?
76
PDB code
5tbk
Structure name
crystal structure of human importin a3 bound to rcc1
Structure deposition date
2016-09-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
6
% buried
60
Peptide accession
O00629
Residue number A
417
Residue number B
456
Peptide name
Importin subunit alpha-3

Ligandability

Cysteine 417 of Importin subunit alpha-3

Cysteine 456 of Importin subunit alpha-3

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