ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Serine/threonine-protein kinase haspin

Intramolecular
Cysteine 467 and cysteine 564
Cysteine 467 and cysteine 478
Cysteine 478 and cysteine 487
Cysteine 478 and cysteine 564
A redox-regulated disulphide may form within Serine/threonine-protein kinase haspin between cysteines 467 and 564. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
7sqm
Structure name
discovery and preclinical pharmacology of ine963, a potent and fast- acting blood-stage antimalarial with a high barrier to resistance and potential for single-dose cure in uncomplicated malaria
Structure deposition date
2021-11-05
Thiol separation (Å)
6
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
69
Peptide accession
Q8TF76
Residue number A
467
Residue number B
564
Peptide name
Serine/threonine-protein kinase haspin

Ligandability

Cysteine 467 of Serine/threonine-protein kinase haspin

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 564 of Serine/threonine-protein kinase haspin

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 haspin between cysteines 467 and 478. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2wb8
Structure name
crystal structure of haspin kinase
Structure deposition date
2009-02-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
12
% buried
73
Peptide accession
Q8TF76
Residue number A
467
Residue number B
478
Peptide name
Serine/threonine-protein kinase haspin

Ligandability

Cysteine 467 of Serine/threonine-protein kinase haspin

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 478 of Serine/threonine-protein kinase haspin

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 haspin between cysteines 478 and 487. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
7sqm
Structure name
discovery and preclinical pharmacology of ine963, a potent and fast- acting blood-stage antimalarial with a high barrier to resistance and potential for single-dose cure in uncomplicated malaria
Structure deposition date
2021-11-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
74
Peptide accession
Q8TF76
Residue number A
478
Residue number B
487
Peptide name
Serine/threonine-protein kinase haspin

Ligandability

Cysteine 478 of Serine/threonine-protein kinase haspin

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 487 of Serine/threonine-protein kinase haspin

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 haspin between cysteines 478 and 564. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
2wb8
Structure name
crystal structure of haspin kinase
Structure deposition date
2009-02-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
73
Peptide accession
Q8TF76
Residue number A
478
Residue number B
564
Peptide name
Serine/threonine-protein kinase haspin

Ligandability

Cysteine 478 of Serine/threonine-protein kinase haspin

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 564 of Serine/threonine-protein kinase haspin

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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