ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Protein O-mannose kinase

Intramolecular
Cysteine 54 and cysteine 67
Cysteine 73 and cysteine 140
Cysteine 202 and cysteine 243
A redox-regulated disulphide may form within Protein O-mannose kinase between cysteines 54 and 67.

Details

Redox score ?
91
PDB code
5gz8
Structure name
crystal structure of catalytic domain of protein o-mannosyl kinase in ligand-free form
Structure deposition date
2016-09-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TUA9
Residue number A
54
Residue number B
67
Peptide name
Protein O-mannose kinase

Ligandability

Cysteine 54 of Protein O-mannose kinase

Cysteine 67 of Protein O-mannose kinase

A redox-regulated disulphide may form within Protein O-mannose kinase between cysteines 73 and 140.

Details

Redox score ?
84
PDB code
5gz8
Structure name
crystal structure of catalytic domain of protein o-mannosyl kinase in ligand-free form
Structure deposition date
2016-09-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TUA9
Residue number A
73
Residue number B
140
Peptide name
Protein O-mannose kinase

Ligandability

Cysteine 73 of Protein O-mannose kinase

Cysteine 140 of Protein O-mannose kinase

A redox-regulated disulphide may form within Protein O-mannose kinase between cysteines 202 and 243.

Details

Redox score ?
84
PDB code
5gz8
Structure name
crystal structure of catalytic domain of protein o-mannosyl kinase in ligand-free form
Structure deposition date
2016-09-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TUA9
Residue number A
202
Residue number B
243
Peptide name
Protein O-mannose kinase

Ligandability

Cysteine 202 of Protein O-mannose kinase

Cysteine 243 of Protein O-mannose kinase

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