ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Serine/threonine-protein kinase Nek1

Intermolecular
Cysteine 163 and cysteine 276
Cysteine 175 and cysteine 276
Intramolecular
Cysteine 163 and cysteine 175
A redox-regulated disulphide may form between two units of Serine/threonine-protein kinase Nek1 at cysteines 163 and 276.

Details

Redox score ?
82
PDB code
4b9d
Structure name
crystal structure of human nima-related kinase 1 (nek1) with inhibitor
Structure deposition date
2012-09-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide A name
Serine/threonine-protein kinase Nek1
Peptide B name
Serine/threonine-protein kinase Nek1
Peptide A accession
Q96PY6
Peptide B accession
Q96PY6
Peptide A residue number
163
Peptide B residue number
276

Ligandability

Cysteine 163 of Serine/threonine-protein kinase Nek1

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 276 of Serine/threonine-protein kinase Nek1

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 between two units of Serine/threonine-protein kinase Nek1 at cysteines 175 and 276. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4apc
Structure name
crystal structure of human nima-related kinase 1 (nek1)
Structure deposition date
2012-04-02
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
nan
Peptide A name
Serine/threonine-protein kinase Nek1
Peptide B name
Serine/threonine-protein kinase Nek1
Peptide A accession
Q96PY6
Peptide B accession
Q96PY6
Peptide A residue number
175
Peptide B residue number
276

Ligandability

Cysteine 175 of Serine/threonine-protein kinase Nek1

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 276 of Serine/threonine-protein kinase Nek1

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 Nek1 between cysteines 163 and 175. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4apc
Structure name
crystal structure of human nima-related kinase 1 (nek1)
Structure deposition date
2012-04-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
34
Peptide accession
Q96PY6
Residue number A
163
Residue number B
175
Peptide name
Serine/threonine-protein kinase Nek1

Ligandability

Cysteine 163 of Serine/threonine-protein kinase Nek1

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 175 of Serine/threonine-protein kinase Nek1

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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