ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Histone deacetylase complex subunit SAP25

Intramolecular
Cysteine 163 and cysteine 181
A redox-regulated disulphide may form within Histone deacetylase complex subunit SAP25 between cysteines 163 and 181. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
2rms
Structure name
solution structure of the msin3a pah1-sap25 sid complex
Structure deposition date
2007-11-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
31
Minimum pKa ?
9
% buried
0
Peptide accession
Q1EHW4
Residue number A
163
Residue number B
181
Peptide name
Histone deacetylase complex subunit SAP25

Ligandability

Cysteine 163 of Histone deacetylase complex subunit SAP25

Cysteine 181 of Histone deacetylase complex subunit SAP25

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