a tool for identifying drug-targetable redox-active disulphides

Beta-chain

Intramolecular

Cysteine 52 and cysteine 120

A redox-regulated disulphide may form within Beta-chain between cysteines 52 and 120 (23 and 91 respectively in this structure).

Details

Redox score ?

82

PDB code

Structure name

crystal structure of staphylococcal enterotoxin g (seg) in complex with a high affinity mutant mouse t-cell receptor chain

Structure deposition date

2010-09-17

Thiol separation (Å)

2

Half-sphere exposure sum ?

86

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

52

Residue number B

120

Peptide name

Beta-chain

Ligandability

Cysteine 52 of Beta-chain

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 120 of Beta-chain

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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