ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ig heavy chain V region M603

Intramolecular
Cysteine 198 and cysteine 222
A redox-regulated disulphide may form within Ig heavy chain V region M603 between cysteines 198 and 222.

Details

Redox score ?
nan
PDB code
1mcp
Structure name
phosphocholine binding immunoglobulin fab mc/pc603
Structure deposition date
1984-07-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01789
Residue number A
198
Residue number B
222
Peptide name
Ig heavy chain V region M603

Ligandability

Cysteine 198 of Ig heavy chain V region M603

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 222 of Ig heavy chain V region M603

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 198 in protein A could not be asigned to a Uniprot residue.
Cysteine 222 in protein B could not be asigned to a Uniprot residue.
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