ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein-tyrosine kinase 6

Intramolecular
Cysteine 408 and cysteine 412
Cysteine 301 and cysteine 433
Cysteine 423 and cysteine 425
A redox-regulated disulphide may form within Protein-tyrosine kinase 6 between cysteines 408 and 412.

Details

Redox score ?
73
PDB code
5d7v
Structure name
crystal structure of ptk6 kinase domain
Structure deposition date
2015-08-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
34
Peptide accession
Q13882
Residue number A
408
Residue number B
412
Peptide name
Protein-tyrosine kinase 6

Ligandability

Cysteine 408 of Protein-tyrosine kinase 6

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 412 of Protein-tyrosine kinase 6

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.

A redox-regulated disulphide may form within Protein-tyrosine kinase 6 between cysteines 301 and 433. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
6cz4
Structure name
structure of the ptk6 kinase domain bound to a type ii inhibitor 2- {[(3r,4s)-3-fluoro-1-{[4-(trifluoromethoxy)phenyl]acetyl}piperidin-4- yl]oxy}-5-(1-methyl-1h-imidazol-4-yl)pyridine-3-carboxamide
Structure deposition date
2018-04-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
9
% buried
35
Peptide accession
Q13882
Residue number A
301
Residue number B
433
Peptide name
Protein-tyrosine kinase 6

Ligandability

Cysteine 301 of Protein-tyrosine kinase 6

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 433 of Protein-tyrosine kinase 6

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.

A redox-regulated disulphide may form within Protein-tyrosine kinase 6 between cysteines 423 and 425. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
5h2u
Structure name
crystal structure of ptk6 kinase domain complexed with dasatinib
Structure deposition date
2016-10-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
60
Peptide accession
Q13882
Residue number A
423
Residue number B
425
Peptide name
Protein-tyrosine kinase 6

Ligandability

Cysteine 423 of Protein-tyrosine kinase 6

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 Protein-tyrosine kinase 6

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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