ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Ras and EF-hand domain-containing protein

Intermolecular
Cysteine 20 and cysteine 20
Intramolecular
Cysteine 20 and cysteine 37
A redox-regulated disulphide may form between two units of Ras and EF-hand domain-containing protein at cysteines 20 and 20. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2pmy
Structure name
ef-hand domain of human rasef
Structure deposition date
2007-04-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide A name
Ras and EF-hand domain-containing protein
Peptide B name
Ras and EF-hand domain-containing protein
Peptide A accession
Q8IZ41
Peptide B accession
Q8IZ41
Peptide A residue number
20
Peptide B residue number
20

Ligandability

A redox-regulated disulphide may form within Ras and EF-hand domain-containing protein between cysteines 20 and 37. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2pmy
Structure name
ef-hand domain of human rasef
Structure deposition date
2007-04-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8IZ41
Residue number A
20
Residue number B
37
Peptide name
Ras and EF-hand domain-containing protein

Ligandability

Cysteine 20 of Ras and EF-hand domain-containing protein

Cysteine 37 of Ras and EF-hand domain-containing protein

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