ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Serine/threonine-protein kinase pim-1

Intramolecular
Cysteine 158 and cysteine 161
Cysteine 237 and cysteine 263
Cysteine 263 and cysteine 270
A redox-regulated disulphide may form within Serine/threonine-protein kinase pim-1 between cysteines 158 and 161. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
6l11
Structure name
crystal structure of ser/thr kinase pim1 in complex with 10-debc derivatives
Structure deposition date
2019-09-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
54
Peptide accession
P11309
Residue number A
158
Residue number B
161
Peptide name
Serine/threonine-protein kinase pim-1

Ligandability

Cysteine 158 of Serine/threonine-protein kinase pim-1

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 161 of Serine/threonine-protein kinase pim-1

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-1 between cysteines 237 and 263. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
6kzi
Structure name
crystal structure of ser/thr kinase pim1 in complex with thioridazine derivatives
Structure deposition date
2019-09-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
66
Peptide accession
P11309
Residue number A
237
Residue number B
263
Peptide name
Serine/threonine-protein kinase pim-1

Ligandability

Cysteine 237 of Serine/threonine-protein kinase pim-1

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 263 of Serine/threonine-protein kinase pim-1

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-1 between cysteines 263 and 270. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
3cy2
Structure name
crystal structure of human proto-oncogene serine threonine kinase (pim1) in complex with a consensus peptide and a beta carboline ligand ii
Structure deposition date
2008-04-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
90
Peptide accession
P11309
Residue number A
263
Residue number B
270
Peptide name
Serine/threonine-protein kinase pim-1

Ligandability

Cysteine 263 of Serine/threonine-protein kinase pim-1

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 270 of Serine/threonine-protein kinase pim-1

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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