a tool for identifying drug-targetable redox-active disulphides

Peroxiredoxin-2

Intermolecular

Cysteine 172 and cysteine 51

A redox-regulated disulphide is known to form between two units of Peroxiredoxin-2 at cysteines 172 and 51.

Details

Redox score ?

86

PDB code

Structure name

human peroxiredoxin 2 oxidized (ss)

Structure deposition date

2016-03-02

Thiol separation (Å)

2

Half-sphere exposure sum ?

56

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Peroxiredoxin-2

Peptide B name

Peroxiredoxin-2

Peptide A accession

Peptide B accession

Peptide A residue number

172

Peptide B residue number

51

Ligandability

Cysteine 172 of Peroxiredoxin-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 51 of Peroxiredoxin-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.

If this tool was useful for finding a disulphide, please cite: