a tool for identifying drug-targetable redox-active disulphides

PR domain zinc finger protein 10

Intramolecular

Cysteine 249 and cysteine 281

A redox-regulated disulphide may form within PR domain zinc finger protein 10 between cysteines 249 and 281 (62 and 94 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

43

PDB code

Structure name

methyltransferase domain of human pr domain-containing protein 10

Structure deposition date

2009-07-31

Thiol separation (Å)

10

Half-sphere exposure sum ?

46

Minimum pK_a ?

9

% buried

24

Peptide accession

Residue number A

249

Residue number B

281

Peptide name

PR domain zinc finger protein 10

Ligandability

Cysteine 249 of PR domain zinc finger protein 10

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 281 of PR domain zinc finger protein 10

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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