ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Inactive tyrosine-protein kinase PEAK1

Intramolecular
Cysteine 1515 and cysteine 1590
Cysteine 1335 and cysteine 1336
Cysteine 1335 and cysteine 1468
Cysteine 1336 and cysteine 1468
A redox-regulated disulphide may form within Inactive tyrosine-protein kinase PEAK1 between cysteines 1515 and 1590.

Details

Redox score ?
72
PDB code
6bhc
Structure name
crystal structure of pseduokinase peak1 (sugen kinase 269)
Structure deposition date
2017-10-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
7
% buried
65
Peptide accession
Q9H792
Residue number A
1515
Residue number B
1590
Peptide name
Inactive tyrosine-protein kinase PEAK1

Ligandability

Cysteine 1515 of Inactive tyrosine-protein kinase PEAK1

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 1590 of Inactive tyrosine-protein kinase PEAK1

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 Inactive tyrosine-protein kinase PEAK1 between cysteines 1335 and 1336. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
6bhc
Structure name
crystal structure of pseduokinase peak1 (sugen kinase 269)
Structure deposition date
2017-10-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
72
Peptide accession
Q9H792
Residue number A
1335
Residue number B
1336
Peptide name
Inactive tyrosine-protein kinase PEAK1

Ligandability

Cysteine 1335 of Inactive tyrosine-protein kinase PEAK1

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 1336 of Inactive tyrosine-protein kinase PEAK1

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 Inactive tyrosine-protein kinase PEAK1 between cysteines 1335 and 1468. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
6bhc
Structure name
crystal structure of pseduokinase peak1 (sugen kinase 269)
Structure deposition date
2017-10-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
50
Peptide accession
Q9H792
Residue number A
1335
Residue number B
1468
Peptide name
Inactive tyrosine-protein kinase PEAK1

Ligandability

Cysteine 1335 of Inactive tyrosine-protein kinase PEAK1

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 1468 of Inactive tyrosine-protein kinase PEAK1

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 Inactive tyrosine-protein kinase PEAK1 between cysteines 1336 and 1468. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6bhc
Structure name
crystal structure of pseduokinase peak1 (sugen kinase 269)
Structure deposition date
2017-10-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
57
Peptide accession
Q9H792
Residue number A
1336
Residue number B
1468
Peptide name
Inactive tyrosine-protein kinase PEAK1

Ligandability

Cysteine 1336 of Inactive tyrosine-protein kinase PEAK1

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 1468 of Inactive tyrosine-protein kinase PEAK1

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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