Glutathione S-transferase Mu 3

Intramolecular

A redox-regulated disulphide may form within Glutathione S-transferase Mu 3 between cysteines 208 and 225 (207 and 224 respectively in this structure).

Details

Redox score ?

PDB code

3gtu

Structure name

ligand-free heterodimeric human glutathione s-transferase m2-3 (ec 2

Structure deposition date

1998-07-29

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

% buried

Peptide accession

P21266

Residue number A

208

Residue number B

225

Peptide name

Glutathione S-transferase Mu 3

Ligandability

Cysteine 208 of Glutathione S-transferase Mu 3

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 225 of Glutathione S-transferase Mu 3

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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