ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ras/Rap GTPase-activating protein SynGAP

Intramolecular
Cysteine 524 and cysteine 546
Cysteine 546 and cysteine 547
Cysteine 524 and cysteine 547
A redox-regulated disulphide may form within Ras/Rap GTPase-activating protein SynGAP between cysteines 524 and 546 (509 and 531 respectively in this structure).

Details

Redox score ?
71
PDB code
3bxj
Structure name
crystal structure of the c2-gap fragment of syngap
Structure deposition date
2008-01-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
8
% buried
67
Peptide accession
Q9QUH6
Residue number A
524
Residue number B
546
Peptide name
Ras/Rap GTPase-activating protein SynGAP

Ligandability

Cysteine 524 of Ras/Rap GTPase-activating protein SynGAP

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 546 of Ras/Rap GTPase-activating protein SynGAP

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 Ras/Rap GTPase-activating protein SynGAP between cysteines 546 and 547 (531 and 532 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3bxj
Structure name
crystal structure of the c2-gap fragment of syngap
Structure deposition date
2008-01-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
69
Minimum pKa ?
8
% buried
82
Peptide accession
Q9QUH6
Residue number A
546
Residue number B
547
Peptide name
Ras/Rap GTPase-activating protein SynGAP

Ligandability

Cysteine 546 of Ras/Rap GTPase-activating protein SynGAP

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 547 of Ras/Rap GTPase-activating protein SynGAP

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 Ras/Rap GTPase-activating protein SynGAP between cysteines 524 and 547 (509 and 532 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3bxj
Structure name
crystal structure of the c2-gap fragment of syngap
Structure deposition date
2008-01-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
13
% buried
86
Peptide accession
Q9QUH6
Residue number A
524
Residue number B
547
Peptide name
Ras/Rap GTPase-activating protein SynGAP

Ligandability

Cysteine 524 of Ras/Rap GTPase-activating protein SynGAP

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 547 of Ras/Rap GTPase-activating protein SynGAP

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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