a tool for identifying drug-targetable redox-active disulphides

Ig heavy chain V region 914

Intramolecular

Cysteine 22 and cysteine 95

A redox-regulated disulphide may form within Ig heavy chain V region 914 between cysteines 22 and 95 (22 and 92 respectively in this structure).

Details

Redox score ?

79

PDB code

Structure name

thermodynamic and structural analyses of hydrolytic mechanism by catalytic antibodies

Structure deposition date

2006-07-13

Thiol separation (Å)

2

Half-sphere exposure sum ?

83

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

22

Residue number B

95

Peptide name

Ig heavy chain V region 914

Ligandability

Cysteine 22 of Ig heavy chain V region 914

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 95 of Ig heavy chain V region 914

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.

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