a tool for identifying drug-targetable redox-active disulphides

Serine/threonine-protein kinase D2

Intramolecular

Cysteine 423 and cysteine 425

A redox-regulated disulphide may form within Serine/threonine-protein kinase D2 between cysteines 423 and 425 (33 and 35 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

46

PDB code

Structure name

solution structure of the ph domain of protein kinase c, d2 type from human

Structure deposition date

2005-05-17

Thiol separation (Å)

9

Half-sphere exposure sum ?

56

Minimum pK_a ?

9

% buried

8

Peptide accession

Residue number A

423

Residue number B

425

Peptide name

Serine/threonine-protein kinase D2

Ligandability

Cysteine 423 of Serine/threonine-protein kinase D2

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 425 of Serine/threonine-protein kinase D2

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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