ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Serine/threonine-protein kinase N1

Intramolecular
Cysteine 762 and cysteine 776
Cysteine 662 and cysteine 762
Cysteine 684 and cysteine 692
A redox-regulated disulphide may form within Serine/threonine-protein kinase N1 between cysteines 762 and 776 (768 and 782 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4otg
Structure name
crystal structure of prk1 catalytic domain in complex with lestaurtinib
Structure deposition date
2014-02-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
78
Peptide accession
Q16512
Residue number A
762
Residue number B
776
Peptide name
Serine/threonine-protein kinase N1

Ligandability

Cysteine 762 of Serine/threonine-protein kinase N1

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 776 of Serine/threonine-protein kinase N1

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 N1 between cysteines 662 and 762 (668 and 768 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
4otg
Structure name
crystal structure of prk1 catalytic domain in complex with lestaurtinib
Structure deposition date
2014-02-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
66
Peptide accession
Q16512
Residue number A
662
Residue number B
762
Peptide name
Serine/threonine-protein kinase N1

Ligandability

Cysteine 662 of Serine/threonine-protein kinase N1

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 762 of Serine/threonine-protein kinase N1

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 N1 between cysteines 684 and 692 (690 and 698 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4otg
Structure name
crystal structure of prk1 catalytic domain in complex with lestaurtinib
Structure deposition date
2014-02-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
98
Peptide accession
Q16512
Residue number A
684
Residue number B
692
Peptide name
Serine/threonine-protein kinase N1

Ligandability

Cysteine 684 of Serine/threonine-protein kinase N1

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 692 of Serine/threonine-protein kinase N1

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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