ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Proline-serine-threonine phosphatase-interacting protein 1

Intermolecular
Cysteine 242 and cysteine 242
Intramolecular
Cysteine 13 and cysteine 213
A redox-regulated disulphide may form between two units of Proline-serine-threonine phosphatase-interacting protein 1 at cysteines 242 and 242. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
7aal
Structure name
crystal structure of the f-bar domain of pstipip1, g258a mutant
Structure deposition date
2020-09-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
14
% buried
86
Peptide A name
Proline-serine-threonine phosphatase-interacting protein 1
Peptide B name
Proline-serine-threonine phosphatase-interacting protein 1
Peptide A accession
O43586
Peptide B accession
O43586
Peptide A residue number
242
Peptide B residue number
242

Ligandability

A redox-regulated disulphide may form within Proline-serine-threonine phosphatase-interacting protein 1 between cysteines 13 and 213. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7aam
Structure name
crystal structure of the f-bar domain of pstipip1 bound to the cth domain of the phosphatase lyp
Structure deposition date
2020-09-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
62
Peptide accession
O43586
Residue number A
13
Residue number B
213
Peptide name
Proline-serine-threonine phosphatase-interacting protein 1

Ligandability

Cysteine 13 of Proline-serine-threonine phosphatase-interacting protein 1

Cysteine 213 of Proline-serine-threonine phosphatase-interacting protein 1

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