a tool for identifying drug-targetable redox-active disulphides

V-alpha FR1

Intramolecular

Cysteine 42 and cysteine 109

A redox-regulated disulphide may form within V-alpha FR1 between cysteines 42 and 109 (23 and 90 respectively in this structure).

Details

Redox score ?

81

PDB code

Structure name

crystal structures of high affinity human t-cell receptors bound to pmhc revealnative diagonal binding geometry tcr clone c5c1 complexed with mhc

Structure deposition date

2007-05-16

Thiol separation (Å)

2

Half-sphere exposure sum ?

84

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

42

Residue number B

109

Peptide name

V-alpha FR1

Ligandability

Cysteine 42 of V-alpha FR1

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 109 of V-alpha FR1

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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