a tool for identifying drug-targetable redox-active disulphides

Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform

Intramolecular

Cysteine 173 and cysteine 185

A redox-regulated disulphide may form within Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform between cysteines 173 and 185 (172 and 184 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

Structure name

the catalytic mechanism of phosphorylase kinase probed by mutational studies

Structure deposition date

1999-08-24

Thiol separation (Å)

8

Half-sphere exposure sum ?

57

Minimum pK_a ?

10

% buried

56

Peptide accession

Residue number A

173

Residue number B

185

Peptide name

Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform

Ligandability

Cysteine 173 of Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart 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 185 of Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart 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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