a tool for identifying drug-targetable redox-active disulphides

Ubiquitin carboxyl-terminal hydrolase 14

Intramolecular

Cysteine 122 and cysteine 203 L

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 14 between cysteines 122 and 203 (121 and 202 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

29

PDB code

Structure name

structure of usp14 bound to ubquitin aldehyde

Structure deposition date

2005-09-07

Thiol separation (Å)

10

Half-sphere exposure sum ?

83

Minimum pK_a ?

12

% buried

100

Peptide accession

Residue number A

122

Residue number B

203

Peptide name

Ubiquitin carboxyl-terminal hydrolase 14

Ligandability

Cysteine 122 of Ubiquitin carboxyl-terminal hydrolase 14

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 203 of Ubiquitin carboxyl-terminal hydrolase 14

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.

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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