ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Serine/threonine-protein kinase PLK1

Intramolecular
Cysteine 572 and cysteine 573 L
Cysteine 372 and cysteine 544
Cysteine 405 and cysteine 544
Cysteine 67 and cysteine 133 L
A redox-regulated disulphide may form within Serine/threonine-protein kinase PLK1 between cysteines 572 and 573.

Details

Redox score ?
62
PDB code
5x3s
Structure name
crystal structure of mouse plk1-pbd in complex with phosphopeptide from hef1 (799-809)
Structure deposition date
2017-02-07
Thiol separation (Å)
6
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
55
Peptide accession
Q07832
Residue number A
572
Residue number B
573
Peptide name
Serine/threonine-protein kinase PLK1

Ligandability

Cysteine 572 of Serine/threonine-protein kinase PLK1

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 573 of Serine/threonine-protein kinase PLK1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Serine/threonine-protein kinase PLK1 between cysteines 372 and 544. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
1q4o
Structure name
the structure of the polo box domain of human plk1
Structure deposition date
2003-08-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
11
% buried
nan
Peptide accession
P53350
Residue number A
372
Residue number B
544
Peptide name
Serine/threonine-protein kinase PLK1

Ligandability

Cysteine 372 of Serine/threonine-protein kinase PLK1

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 544 of Serine/threonine-protein kinase PLK1

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 PLK1 between cysteines 405 and 544. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5dms
Structure name
mouse polo-box domain and emi2 (169-177)
Structure deposition date
2015-09-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
9
% buried
68
Peptide accession
Q07832
Residue number A
405
Residue number B
544
Peptide name
Serine/threonine-protein kinase PLK1

Ligandability

Cysteine 405 of Serine/threonine-protein kinase PLK1

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 544 of Serine/threonine-protein kinase PLK1

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 PLK1 between cysteines 67 and 133. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
2owb
Structure name
structure of the catalytic domain of human polo-like kinase 1
Structure deposition date
2007-02-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
12
% buried
92
Peptide accession
P53350
Residue number A
67
Residue number B
133
Peptide name
Serine/threonine-protein kinase PLK1

Ligandability

Cysteine 67 of Serine/threonine-protein kinase PLK1

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 133 of Serine/threonine-protein kinase PLK1

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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