ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Hematopoietic SH2 domain-containing protein

Intramolecular
Cysteine 77 and cysteine 78
Cysteine 77 and cysteine 125
A redox-regulated disulphide may form within Hematopoietic SH2 domain-containing protein between cysteines 77 and 78 (61 and 62 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
2cs0
Structure name
solution structure of the sh2 domain of human hsh2d protein
Structure deposition date
2005-05-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
34
Peptide accession
Q96JZ2
Residue number A
77
Residue number B
78
Peptide name
Hematopoietic SH2 domain-containing protein

Ligandability

Cysteine 77 of Hematopoietic SH2 domain-containing protein

Cysteine 78 of Hematopoietic SH2 domain-containing protein

A redox-regulated disulphide may form within Hematopoietic SH2 domain-containing protein between cysteines 77 and 125 (61 and 109 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2cs0
Structure name
solution structure of the sh2 domain of human hsh2d protein
Structure deposition date
2005-05-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
38
Peptide accession
Q96JZ2
Residue number A
77
Residue number B
125
Peptide name
Hematopoietic SH2 domain-containing protein

Ligandability

Cysteine 77 of Hematopoietic SH2 domain-containing protein

Cysteine 125 of Hematopoietic SH2 domain-containing protein

If this tool was useful for finding a disulphide, please cite: