a tool for identifying drug-targetable redox-active disulphides

Ribosyldihydronicotinamide dehydrogenase [quinone]

Intramolecular

Cysteine 122 and cysteine 180

A redox-regulated disulphide may form within Ribosyldihydronicotinamide dehydrogenase [quinone] between cysteines 122 and 180 (121 and 179 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

26

PDB code

Structure name

structure of the human quinone reductase 2 (nqo2) in complex with pacritinib

Structure deposition date

2016-06-17

Thiol separation (Å)

10

Half-sphere exposure sum ?

81

Minimum pK_a ?

12

% buried

100

Peptide accession

Residue number A

122

Residue number B

180

Peptide name

Ribosyldihydronicotinamide dehydrogenase [quinone]

Ligandability

Cysteine 122 of Ribosyldihydronicotinamide dehydrogenase [quinone]

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 180 of Ribosyldihydronicotinamide dehydrogenase [quinone]

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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