a tool for identifying drug-targetable redox-active disulphides

Spectrin beta chain, non-erythrocytic 2

Intramolecular

Cysteine 2226 and cysteine 2248

A redox-regulated disulphide may form within Spectrin beta chain, non-erythrocytic 2 between cysteines 2226 and 2248 (15 and 37 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

30

PDB code

Structure name

solution structure of pleckstrin homology domain of human beta iii spectrin

Structure deposition date

2004-05-29

Thiol separation (Å)

10

Half-sphere exposure sum ?

74

Minimum pK_a ?

10

% buried

69

Peptide accession

Residue number A

2226

Residue number B

2248

Peptide name

Spectrin beta chain, non-erythrocytic 2

Ligandability

Cysteine 2226 of Spectrin beta chain, non-erythrocytic 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 2248 of Spectrin beta chain, non-erythrocytic 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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