ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

tRNA selenocysteine 1-associated protein 1

Intramolecular
Cysteine 123 and cysteine 157
A redox-regulated disulphide may form within tRNA selenocysteine 1-associated protein 1 between cysteines 123 and 157. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2dhg
Structure name
solution structure of the c-terminal rna recognition motif in trna selenocysteine associated protein
Structure deposition date
2006-03-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
11
% buried
45
Peptide accession
Q9NX07
Residue number A
123
Residue number B
157
Peptide name
tRNA selenocysteine 1-associated protein 1

Ligandability

Cysteine 123 of tRNA selenocysteine 1-associated protein 1

Cysteine 157 of tRNA selenocysteine 1-associated protein 1

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