ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tyrosine-protein phosphatase non-receptor type substrate 1

Intramolecular
Cysteine 170 and cysteine 228
Cysteine 273 and cysteine 331
Cysteine 55 and cysteine 121
A redox-regulated disulphide may form within Tyrosine-protein phosphatase non-receptor type substrate 1 between cysteines 170 and 228 (139 and 197 respectively in this structure).

Details

Redox score ?
81
PDB code
2wng
Structure name
complete extracellular structure of human signal regulatory protein (sirp) alpha
Structure deposition date
2009-07-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78324
Residue number A
170
Residue number B
228
Peptide name
Tyrosine-protein phosphatase non-receptor type substrate 1

Ligandability

Cysteine 170 of Tyrosine-protein phosphatase non-receptor type substrate 1

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 228 of Tyrosine-protein phosphatase non-receptor type substrate 1

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 Tyrosine-protein phosphatase non-receptor type substrate 1 between cysteines 273 and 331 (242 and 300 respectively in this structure).

Details

Redox score ?
81
PDB code
2wng
Structure name
complete extracellular structure of human signal regulatory protein (sirp) alpha
Structure deposition date
2009-07-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78324
Residue number A
273
Residue number B
331
Peptide name
Tyrosine-protein phosphatase non-receptor type substrate 1

Ligandability

Cysteine 273 of Tyrosine-protein phosphatase non-receptor type substrate 1

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 331 of Tyrosine-protein phosphatase non-receptor type substrate 1

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 Tyrosine-protein phosphatase non-receptor type substrate 1 between cysteines 55 and 121 (25 and 91 respectively in this structure).

Details

Redox score ?
81
PDB code
6bit
Structure name
sirpalpha antibody complex
Structure deposition date
2017-11-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78324
Residue number A
55
Residue number B
121
Peptide name
Tyrosine-protein phosphatase non-receptor type substrate 1

Ligandability

Cysteine 55 of Tyrosine-protein phosphatase non-receptor type substrate 1

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 121 of Tyrosine-protein phosphatase non-receptor type substrate 1

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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