ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tyrosine-protein kinase CSK

Intramolecular
Cysteine 122 and cysteine 164 L
Cysteine 299 and cysteine 422
Cysteine 119 and cysteine 164
A redox-regulated disulphide may form within Tyrosine-protein kinase CSK between cysteines 122 and 164.

Details

Redox score ?
83
PDB code
3eac
Structure name
crystal structure of sh2 domain of human csk (carboxyl-terminal src kinase), oxidized form
Structure deposition date
2008-08-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P41240
Residue number A
122
Residue number B
164
Peptide name
Tyrosine-protein kinase CSK

Ligandability

Cysteine 122 of Tyrosine-protein kinase CSK

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 164 of Tyrosine-protein kinase CSK

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 kinase CSK between cysteines 299 and 422. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3d7u
Structure name
structural basis for the recognition of c-src by its inactivator csk
Structure deposition date
2008-05-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
98
Peptide accession
P41240
Residue number A
299
Residue number B
422
Peptide name
Tyrosine-protein kinase CSK

Ligandability

Cysteine 299 of Tyrosine-protein kinase CSK

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 422 of Tyrosine-protein kinase CSK

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 kinase CSK between cysteines 119 and 164. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
2rsy
Structure name
solution structure of the sh2 domain of csk in complex with a phosphopeptide from cbp
Structure deposition date
2012-09-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
nan
Peptide accession
P32577
Residue number A
119
Residue number B
164
Peptide name
Tyrosine-protein kinase CSK

Ligandability

Cysteine 119 of Tyrosine-protein kinase CSK

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 164 of Tyrosine-protein kinase CSK

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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