a tool for identifying drug-targetable redox-active disulphides

Butyrophilin-like protein 2

Intramolecular

Cysteine 50 and cysteine 124

A redox-regulated disulphide may form within Butyrophilin-like protein 2 between cysteines 50 and 124 (24 and 98 respectively in this structure).

Details

Redox score ?

81

PDB code

Structure name

solution nmr structure of the n-terminal immunoglobulin variable domain of btnl2

Structure deposition date

2019-11-03

Thiol separation (Å)

2

Half-sphere exposure sum ?

80

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

50

Residue number B

124

Peptide name

Butyrophilin-like protein 2

Ligandability

Cysteine 50 of Butyrophilin-like protein 2

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 124 of Butyrophilin-like protein 2

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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