ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Torsin-1A

Intramolecular
Cysteine 280 and cysteine 319
Cysteine 320 and cysteine 50
A redox-regulated disulphide may form within Torsin-1A between cysteines 280 and 319.

Details

Redox score ?
74
PDB code
5j1s
Structure name
torsina-lull1 complex, h
Structure deposition date
2016-03-29
Thiol separation (Å)
3
Half-sphere exposure sum ?
78
Minimum pKa ?
9
% buried
100
Peptide accession
O14656
Residue number A
280
Residue number B
319
Peptide name
Torsin-1A

Ligandability

Cysteine 280 of Torsin-1A

Cysteine 319 of Torsin-1A

A redox-regulated disulphide may form within Torsin-1A between cysteines 320 and 50 (320 and 349 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6fv0
Structure name
crystal structure of the tpr domain of klc1 in complex with the c- terminal peptide of torsina
Structure deposition date
2018-02-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
80
Peptide accession
Q9ER39
Residue number A
320
Residue number B
50
Peptide name
Torsin-1A

Ligandability

Cysteine 320 of Torsin-1A

Cysteine 50 of Torsin-1A

Cysteine 320 in protein A could not be asigned to a Uniprot residue.
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