a tool for identifying drug-targetable redox-active disulphides

Aldehyde dehydrogenase, cytosolic 1

Intramolecular

Cysteine 185 and cysteine 186

A redox-regulated disulphide may form within Aldehyde dehydrogenase, cytosolic 1 between cysteines 185 and 186 (184 and 185 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

58

PDB code

Structure name

the x-ray crystal structure of eta-crystallin

Structure deposition date

2002-12-15

Thiol separation (Å)

4

Half-sphere exposure sum ?

98

Minimum pK_a ?

10

% buried

100

Peptide accession

Residue number A

185

Residue number B

186

Peptide name

Aldehyde dehydrogenase, cytosolic 1

Ligandability

Cysteine 185 of Aldehyde dehydrogenase, cytosolic 1

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 186 of Aldehyde dehydrogenase, cytosolic 1

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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