a tool for identifying drug-targetable redox-active disulphides

Protein S100-A14

Intermolecular

Cysteine 62 and cysteine 4

A redox-regulated disulphide may form between two units of Protein S100-A14 at cysteines 62 and 4 (62 and 108 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

56

PDB code

Structure name

solution structure and dynamics of human s100a14

Structure deposition date

2012-11-05

Thiol separation (Å)

9

Half-sphere exposure sum ?

20

Minimum pK_a ?

9

% buried

0

Peptide A name

Protein S100-A14

Peptide B name

Protein S100-A14

Peptide A accession

Peptide B accession

Peptide A residue number

62

Peptide B residue number

4

Ligandability

Cysteine 62 of Protein S100-A14

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 4 of Protein S100-A14

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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