ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Putative tyrosine-protein phosphatase auxilin

Intramolecular
Cysteine 142 and cysteine 179
Cysteine 157 and cysteine 179
Cysteine 142 and cysteine 157
A redox-regulated disulphide may form within Putative tyrosine-protein phosphatase auxilin between cysteines 142 and 179. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
3n0a
Structure name
crystal structure of auxilin (40-400)
Structure deposition date
2010-05-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
13
% buried
100
Peptide accession
Q27974
Residue number A
142
Residue number B
179
Peptide name
Putative tyrosine-protein phosphatase auxilin

Ligandability

Cysteine 142 of Putative tyrosine-protein phosphatase auxilin

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 179 of Putative tyrosine-protein phosphatase auxilin

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 Putative tyrosine-protein phosphatase auxilin between cysteines 157 and 179. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
3n0a
Structure name
crystal structure of auxilin (40-400)
Structure deposition date
2010-05-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
13
% buried
100
Peptide accession
Q27974
Residue number A
157
Residue number B
179
Peptide name
Putative tyrosine-protein phosphatase auxilin

Ligandability

Cysteine 157 of Putative tyrosine-protein phosphatase auxilin

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 179 of Putative tyrosine-protein phosphatase auxilin

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 Putative tyrosine-protein phosphatase auxilin between cysteines 142 and 157. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
3n0a
Structure name
crystal structure of auxilin (40-400)
Structure deposition date
2010-05-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
13
% buried
100
Peptide accession
Q27974
Residue number A
142
Residue number B
157
Peptide name
Putative tyrosine-protein phosphatase auxilin

Ligandability

Cysteine 142 of Putative tyrosine-protein phosphatase auxilin

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 157 of Putative tyrosine-protein phosphatase auxilin

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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