a tool for identifying drug-targetable redox-active disulphides

Catenin alpha-2

Intramolecular

Cysteine 766 and cysteine 771

A redox-regulated disulphide may form within Catenin alpha-2 between cysteines 766 and 771.

Details

Redox score ?

70

PDB code

Structure name

crystal structure of the alpha-n-catenin actin-binding domain h1 mutant

Structure deposition date

2018-06-22

Thiol separation (Å)

5

Half-sphere exposure sum ?

61

Minimum pK_a ?

10

% buried

24

Peptide accession

Residue number A

766

Residue number B

771

Peptide name

Catenin alpha-2

Ligandability

Cysteine 766 of Catenin alpha-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 771 of Catenin alpha-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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