a tool for identifying drug-targetable redox-active disulphides

L-xylulose reductase

Intramolecular

Cysteine 138 and cysteine 150 L

A redox-regulated disulphide may form within L-xylulose reductase between cysteines 138 and 150.

Details

Redox score ?

77

PDB code

Structure name

structure of the tetrameric form of human l-xylulose reductase

Structure deposition date

2004-08-09

Thiol separation (Å)

2

Half-sphere exposure sum ?

88

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

138

Residue number B

150

Peptide name

L-xylulose reductase

Ligandability

Cysteine 138 of L-xylulose reductase

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 150 of L-xylulose reductase

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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