ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Serine/threonine-protein phosphatase 2A activator

Intramolecular
Cysteine 199 and cysteine 202
Cysteine 199 and cysteine 200
Cysteine 200 and cysteine 202
A redox-regulated disulphide may form within Serine/threonine-protein phosphatase 2A activator between cysteines 199 and 202 (164 and 167 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
2hv7
Structure name
crystal structure of phosphotyrosyl phosphatase activator bound to atpgammas
Structure deposition date
2006-07-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
78
Peptide accession
Q15257
Residue number A
199
Residue number B
202
Peptide name
Serine/threonine-protein phosphatase 2A activator

Ligandability

Cysteine 199 of Serine/threonine-protein phosphatase 2A activator

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 202 of Serine/threonine-protein phosphatase 2A activator

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Serine/threonine-protein phosphatase 2A activator between cysteines 199 and 200 (164 and 165 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
2ixm
Structure name
structure of human ptpa
Structure deposition date
2006-07-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
96
Peptide accession
Q15257
Residue number A
199
Residue number B
200
Peptide name
Serine/threonine-protein phosphatase 2A activator

Ligandability

Cysteine 199 of Serine/threonine-protein phosphatase 2A activator

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 200 of Serine/threonine-protein phosphatase 2A activator

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Serine/threonine-protein phosphatase 2A activator between cysteines 200 and 202 (165 and 167 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
2hv7
Structure name
crystal structure of phosphotyrosyl phosphatase activator bound to atpgammas
Structure deposition date
2006-07-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
78
Peptide accession
Q15257
Residue number A
200
Residue number B
202
Peptide name
Serine/threonine-protein phosphatase 2A activator

Ligandability

Cysteine 200 of Serine/threonine-protein phosphatase 2A activator

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 202 of Serine/threonine-protein phosphatase 2A activator

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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