a tool for identifying drug-targetable redox-active disulphides

Glutathione peroxidase 6

Intramolecular

Cysteine 32 and cysteine 156

A redox-regulated disulphide may form within Glutathione peroxidase 6 between cysteines 32 and 156.

Details

Redox score ?

85

PDB code

Structure name

crystal structure of gpx6

Structure deposition date

2021-07-13

Thiol separation (Å)

2

Half-sphere exposure sum ?

64

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

32

Residue number B

156

Peptide name

Glutathione peroxidase 6

Ligandability

Cysteine 32 of Glutathione peroxidase 6

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 156 of Glutathione peroxidase 6

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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