ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein mono-ADP-ribosyltransferase PARP9

Intramolecular
Cysteine 413 and cysteine 417
A redox-regulated disulphide may form within Protein mono-ADP-ribosyltransferase PARP9 between cysteines 413 and 417 (378 and 382 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
5ail
Structure name
human parp9 2nd macrodomain
Structure deposition date
2015-02-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
13
% buried
97
Peptide accession
Q8IXQ6
Residue number A
413
Residue number B
417
Peptide name
Protein mono-ADP-ribosyltransferase PARP9

Ligandability

Cysteine 413 of Protein mono-ADP-ribosyltransferase PARP9

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 417 of Protein mono-ADP-ribosyltransferase PARP9

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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