a tool for identifying drug-targetable redox-active disulphides

Serine/threonine-protein kinase LMTK3

Intramolecular

Cysteine 196 and cysteine 200

A redox-regulated disulphide may form within Serine/threonine-protein kinase LMTK3 between cysteines 196 and 200 (225 and 229 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

lemur tyrosine kinase 3 (lmtk3)

Structure deposition date

2019-07-30

Thiol separation (Å)

9

Half-sphere exposure sum ?

60

Minimum pK_a ?

10

% buried

40

Peptide accession

Residue number A

196

Residue number B

200

Peptide name

Serine/threonine-protein kinase LMTK3

Ligandability

Cysteine 196 of Serine/threonine-protein kinase LMTK3

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 200 of Serine/threonine-protein kinase LMTK3

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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