ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Serine/threonine-protein kinase WNK3

Intramolecular
Cysteine 278 and cysteine 337
Cysteine 176 and cysteine 222
Cysteine 254 and cysteine 337
Cysteine 254 and cysteine 278
Cysteine 254 and cysteine 385
Cysteine 337 and cysteine 385
A redox-regulated disulphide may form within Serine/threonine-protein kinase WNK3 between cysteines 278 and 337.

Details

Redox score ?
65
PDB code
5o2c
Structure name
crystal structure of wnk3 kinase and cct1 didomain in a unphosphorylated state
Structure deposition date
2017-05-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
86
Minimum pKa ?
10
% buried
100
Peptide accession
Q9BYP7
Residue number A
278
Residue number B
337
Peptide name
Serine/threonine-protein kinase WNK3

Ligandability

Cysteine 278 of Serine/threonine-protein kinase WNK3

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 337 of Serine/threonine-protein kinase WNK3

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 Serine/threonine-protein kinase WNK3 between cysteines 176 and 222. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5o2b
Structure name
crystal structure of wnk3 kinase domain in a diphosphorylated state and in a complex with the inhibitor pp-121
Structure deposition date
2017-05-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
52
Peptide accession
Q9BYP7
Residue number A
176
Residue number B
222
Peptide name
Serine/threonine-protein kinase WNK3

Ligandability

Cysteine 176 of Serine/threonine-protein kinase WNK3

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 222 of Serine/threonine-protein kinase WNK3

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 Serine/threonine-protein kinase WNK3 between cysteines 254 and 337. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
5o2c
Structure name
crystal structure of wnk3 kinase and cct1 didomain in a unphosphorylated state
Structure deposition date
2017-05-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
10
% buried
100
Peptide accession
Q9BYP7
Residue number A
254
Residue number B
337
Peptide name
Serine/threonine-protein kinase WNK3

Ligandability

Cysteine 254 of Serine/threonine-protein kinase WNK3

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 337 of Serine/threonine-protein kinase WNK3

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 Serine/threonine-protein kinase WNK3 between cysteines 254 and 278. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
5o21
Structure name
crystal structure of wnk3 kinase domain in a monophosphorylated state with chloride bound in the active site
Structure deposition date
2017-05-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
100
Peptide accession
Q9BYP7
Residue number A
254
Residue number B
278
Peptide name
Serine/threonine-protein kinase WNK3

Ligandability

Cysteine 254 of Serine/threonine-protein kinase WNK3

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 278 of Serine/threonine-protein kinase WNK3

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 Serine/threonine-protein kinase WNK3 between cysteines 254 and 385. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
5o2b
Structure name
crystal structure of wnk3 kinase domain in a diphosphorylated state and in a complex with the inhibitor pp-121
Structure deposition date
2017-05-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
100
Peptide accession
Q9BYP7
Residue number A
254
Residue number B
385
Peptide name
Serine/threonine-protein kinase WNK3

Ligandability

Cysteine 254 of Serine/threonine-protein kinase WNK3

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 385 of Serine/threonine-protein kinase WNK3

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 Serine/threonine-protein kinase WNK3 between cysteines 337 and 385. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
5o26
Structure name
crystal structure of wnk3 kinase domain in a diphosphorylated state and in complex with amp-pnp/mg2+
Structure deposition date
2017-05-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
100
Peptide accession
Q9BYP7
Residue number A
337
Residue number B
385
Peptide name
Serine/threonine-protein kinase WNK3

Ligandability

Cysteine 337 of Serine/threonine-protein kinase WNK3

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 385 of Serine/threonine-protein kinase WNK3

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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