ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Growth factor receptor-bound protein 10

Intramolecular
Cysteine 534 and cysteine 583
Cysteine 561 and cysteine 616
Cysteine 313 and cysteine 321
Cysteine 194 and cysteine 223
A redox-regulated disulphide may form within Growth factor receptor-bound protein 10 between cysteines 534 and 583 (476 and 525 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
1nrv
Structure name
crystal structure of the sh2 domain of grb10
Structure deposition date
2003-01-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
36
Peptide accession
Q13322
Residue number A
534
Residue number B
583
Peptide name
Growth factor receptor-bound protein 10

Ligandability

Cysteine 534 of Growth factor receptor-bound protein 10

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 583 of Growth factor receptor-bound protein 10

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 Growth factor receptor-bound protein 10 between cysteines 561 and 616 (476 and 531 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
3m7f
Structure name
crystal structure of the nedd4 c2/grb10 sh2 complex
Structure deposition date
2010-03-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
46
Peptide accession
Q60760
Residue number A
561
Residue number B
616
Peptide name
Growth factor receptor-bound protein 10

Ligandability

Cysteine 561 of Growth factor receptor-bound protein 10

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 616 of Growth factor receptor-bound protein 10

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 Growth factor receptor-bound protein 10 between cysteines 313 and 321 (255 and 263 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
3hk0
Structure name
crystal structure of the ra and ph domains of grb10
Structure deposition date
2009-05-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
46
Peptide accession
Q13322
Residue number A
313
Residue number B
321
Peptide name
Growth factor receptor-bound protein 10

Ligandability

Cysteine 313 of Growth factor receptor-bound protein 10

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 321 of Growth factor receptor-bound protein 10

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 Growth factor receptor-bound protein 10 between cysteines 194 and 223 (136 and 165 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
3hk0
Structure name
crystal structure of the ra and ph domains of grb10
Structure deposition date
2009-05-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
85
Peptide accession
Q13322
Residue number A
194
Residue number B
223
Peptide name
Growth factor receptor-bound protein 10

Ligandability

Cysteine 194 of Growth factor receptor-bound protein 10

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 223 of Growth factor receptor-bound protein 10

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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