ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Probable ATP-dependent RNA helicase DDX53

Intramolecular
Cysteine 316 and cysteine 328
A redox-regulated disulphide may form within Probable ATP-dependent RNA helicase DDX53 between cysteines 316 and 328 (325 and 337 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3iuy
Structure name
crystal structure of ddx53 dead-box domain
Structure deposition date
2009-08-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
60
Peptide accession
Q86TM3
Residue number A
316
Residue number B
328
Peptide name
Probable ATP-dependent RNA helicase DDX53

Ligandability

Cysteine 316 of Probable ATP-dependent RNA helicase DDX53

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 328 of Probable ATP-dependent RNA helicase DDX53

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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