ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tyrosine-protein kinase

Intramolecular
Cysteine 485 and cysteine 489
Cysteine 485 and cysteine 498
Cysteine 489 and cysteine 498
Cysteine 498 and cysteine 500
A redox-regulated disulphide may form within Tyrosine-protein kinase between cysteines 485 and 489 (483 and 487 respectively in this structure).

Details

Redox score ?
74
PDB code
6f3f
Structure name
autoinhibited src kinase bound to adp
Structure deposition date
2017-11-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
10
% buried
28
Peptide accession
Q3UKD6
Residue number A
485
Residue number B
489
Peptide name
Tyrosine-protein kinase

Ligandability

Cysteine 485 of Tyrosine-protein kinase

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 489 of Tyrosine-protein kinase

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 Tyrosine-protein kinase between cysteines 485 and 498 (483 and 496 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
6f3f
Structure name
autoinhibited src kinase bound to adp
Structure deposition date
2017-11-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
22
Peptide accession
Q3UKD6
Residue number A
485
Residue number B
498
Peptide name
Tyrosine-protein kinase

Ligandability

Cysteine 485 of Tyrosine-protein kinase

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 498 of Tyrosine-protein kinase

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 Tyrosine-protein kinase between cysteines 489 and 498 (487 and 496 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6f3f
Structure name
autoinhibited src kinase bound to adp
Structure deposition date
2017-11-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
43
Peptide accession
Q3UKD6
Residue number A
489
Residue number B
498
Peptide name
Tyrosine-protein kinase

Ligandability

Cysteine 489 of Tyrosine-protein kinase

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 498 of Tyrosine-protein kinase

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 Tyrosine-protein kinase between cysteines 498 and 500 (496 and 498 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
6f3f
Structure name
autoinhibited src kinase bound to adp
Structure deposition date
2017-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
68
Peptide accession
Q3UKD6
Residue number A
498
Residue number B
500
Peptide name
Tyrosine-protein kinase

Ligandability

Cysteine 498 of Tyrosine-protein kinase

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 500 of Tyrosine-protein kinase

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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