a tool for identifying drug-targetable redox-active disulphides

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform

Intramolecular

Cysteine 49 and cysteine 50

A redox-regulated disulphide may form within Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform between cysteines 49 and 50. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

42

PDB code

Structure name

crystal structure of a protein phosphatase 2a (pp2a) holoenzyme

Structure deposition date

2006-09-07

Thiol separation (Å)

9

Half-sphere exposure sum ?

56

Minimum pK_a ?

9

% buried

30

Peptide accession

Residue number A

49

Residue number B

50

Peptide name

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform

Ligandability

Cysteine 49 of Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform

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 50 of Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform

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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