Glutathione synthetase

Intramolecular

A redox-regulated disulphide may form within Glutathione synthetase between cysteines 409 and 422. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2hgs

Structure name

human glutathione synthetase

Structure deposition date

1999-01-04

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

P48637

Residue number A

409

Residue number B

422

Peptide name

Glutathione synthetase

Ligandability

Cysteine 409 of Glutathione synthetase

Not ligandable in the dataset of Yang et al.

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 422 of Glutathione synthetase

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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