Serine/threonine-protein kinase 16

Intramolecular

A redox-regulated disulphide may form within Serine/threonine-protein kinase 16 between cysteines 174 and 210. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2buj

Structure name

crystal structure of the human serine-threonine kinase 16 in complex with staurosporine

Structure deposition date

2005-06-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

O75716

Residue number A

174

Residue number B

210

Peptide name

Serine/threonine-protein kinase 16

Ligandability

Cysteine 174 of Serine/threonine-protein kinase 16

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.