ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Serine/threonine-protein kinase pim-2

Intramolecular
Cysteine 259 and cysteine 260
Cysteine 233 and cysteine 260
Cysteine 233 and cysteine 259
Cysteine 142 and cysteine 177 L
Cysteine 259 and cysteine 266
A redox-regulated disulphide may form within Serine/threonine-protein kinase pim-2 between cysteines 259 and 260. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
4x7q
Structure name
pim2 kinase in complex with compound 1s
Structure deposition date
2014-12-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
37
Peptide accession
Q9P1W9
Residue number A
259
Residue number B
260
Peptide name
Serine/threonine-protein kinase pim-2

Ligandability

Cysteine 259 of Serine/threonine-protein kinase pim-2

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 260 of Serine/threonine-protein kinase pim-2

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 pim-2 between cysteines 233 and 260. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
2iwi
Structure name
crystal structure of the human pim2 in complex with a ruthenium organometallic ligand ru1
Structure deposition date
2006-06-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P1W9
Residue number A
233
Residue number B
260
Peptide name
Serine/threonine-protein kinase pim-2

Ligandability

Cysteine 233 of Serine/threonine-protein kinase pim-2

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 260 of Serine/threonine-protein kinase pim-2

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 pim-2 between cysteines 233 and 259. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4x7q
Structure name
pim2 kinase in complex with compound 1s
Structure deposition date
2014-12-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
56
Peptide accession
Q9P1W9
Residue number A
233
Residue number B
259
Peptide name
Serine/threonine-protein kinase pim-2

Ligandability

Cysteine 233 of Serine/threonine-protein kinase pim-2

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 259 of Serine/threonine-protein kinase pim-2

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 pim-2 between cysteines 142 and 177. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2iwi
Structure name
crystal structure of the human pim2 in complex with a ruthenium organometallic ligand ru1
Structure deposition date
2006-06-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P1W9
Residue number A
142
Residue number B
177
Peptide name
Serine/threonine-protein kinase pim-2

Ligandability

Cysteine 142 of Serine/threonine-protein kinase pim-2

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.

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 177 of Serine/threonine-protein kinase pim-2

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 pim-2 between cysteines 259 and 266. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4x7q
Structure name
pim2 kinase in complex with compound 1s
Structure deposition date
2014-12-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
80
Peptide accession
Q9P1W9
Residue number A
259
Residue number B
266
Peptide name
Serine/threonine-protein kinase pim-2

Ligandability

Cysteine 259 of Serine/threonine-protein kinase pim-2

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 266 of Serine/threonine-protein kinase pim-2

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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