ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Ig heavy chain V region J558

Intramolecular
Cysteine 22 and cysteine 196
A redox-regulated disulphide may form within Ig heavy chain V region J558 between cysteines 22 and 196 (141 and 196 respectively in this structure).

Details

Redox score ?
nan
PDB code
2oz4
Structure name
structural plasticity in igsf domain 4 of icam-1 mediates cell surface dimerization
Structure deposition date
2007-02-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01757
Residue number A
22
Residue number B
196
Peptide name
Ig heavy chain V region J558

Ligandability

Cysteine 22 of Ig heavy chain V region J558

Cysteine 196 of Ig heavy chain V region J558

Cysteine 196 in protein B could not be asigned to a Uniprot residue.
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