ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Rac GTPase-activating protein 1

Intramolecular
Cysteine 316 and cysteine 319
Cysteine 316 and cysteine 335 L
Cysteine 319 and cysteine 335 L
Cysteine 300 and cysteine 327 L
Cysteine 300 and cysteine 303 L
Cysteine 303 and cysteine 327
Cysteine 300 and cysteine 331 L
Cysteine 316 and cysteine 331 L
Cysteine 16 and cysteine 109
Cysteine 327 and cysteine 331 L
More...
Cysteine 319 and cysteine 331 L
Cysteine 303 and cysteine 331 L
Cysteine 331 and cysteine 335 L
Cysteine 369 and cysteine 419
Cysteine 109 and cysteine 159
Cysteine 16 and cysteine 159
A redox-regulated disulphide may form within Rac GTPase-activating protein 1 between cysteines 316 and 319.

Details

Redox score ?
94
PDB code
4b6d
Structure name
structure of the atypical c1 domain of mgcracgap
Structure deposition date
2012-08-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
2
% buried
41
Peptide accession
Q9H0H5
Residue number A
316
Residue number B
319
Peptide name
Rac GTPase-activating protein 1

Ligandability

Cysteine 316 of Rac GTPase-activating protein 1

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 319 of Rac GTPase-activating protein 1

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 Rac GTPase-activating protein 1 between cysteines 316 and 335.

Details

Redox score ?
93
PDB code
4b6d
Structure name
structure of the atypical c1 domain of mgcracgap
Structure deposition date
2012-08-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
1
% buried
46
Peptide accession
Q9H0H5
Residue number A
316
Residue number B
335
Peptide name
Rac GTPase-activating protein 1

Ligandability

Cysteine 316 of Rac GTPase-activating protein 1

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 335 of Rac GTPase-activating protein 1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Rac GTPase-activating protein 1 between cysteines 319 and 335.

Details

Redox score ?
88
PDB code
4b6d
Structure name
structure of the atypical c1 domain of mgcracgap
Structure deposition date
2012-08-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
2
% buried
50
Peptide accession
Q9H0H5
Residue number A
319
Residue number B
335
Peptide name
Rac GTPase-activating protein 1

Ligandability

Cysteine 319 of Rac GTPase-activating protein 1

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 335 of Rac GTPase-activating protein 1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Rac GTPase-activating protein 1 between cysteines 300 and 327.

Details

Redox score ?
79
PDB code
4b6d
Structure name
structure of the atypical c1 domain of mgcracgap
Structure deposition date
2012-08-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
22
Peptide accession
Q9H0H5
Residue number A
300
Residue number B
327
Peptide name
Rac GTPase-activating protein 1

Ligandability

Cysteine 300 of Rac GTPase-activating protein 1

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 327 of Rac GTPase-activating protein 1

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 Rac GTPase-activating protein 1 between cysteines 300 and 303.

Details

Redox score ?
76
PDB code
4b6d
Structure name
structure of the atypical c1 domain of mgcracgap
Structure deposition date
2012-08-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
7
% buried
42
Peptide accession
Q9H0H5
Residue number A
300
Residue number B
303
Peptide name
Rac GTPase-activating protein 1

Ligandability

Cysteine 300 of Rac GTPase-activating protein 1

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 303 of Rac GTPase-activating protein 1

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 Rac GTPase-activating protein 1 between cysteines 303 and 327.

Details

Redox score ?
75
PDB code
4b6d
Structure name
structure of the atypical c1 domain of mgcracgap
Structure deposition date
2012-08-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
39
Peptide accession
Q9H0H5
Residue number A
303
Residue number B
327
Peptide name
Rac GTPase-activating protein 1

Ligandability

Cysteine 303 of Rac GTPase-activating protein 1

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 327 of Rac GTPase-activating protein 1

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 Rac GTPase-activating protein 1 between cysteines 300 and 331. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
4b6d
Structure name
structure of the atypical c1 domain of mgcracgap
Structure deposition date
2012-08-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
nan
Peptide accession
Q9H0H5
Residue number A
300
Residue number B
331
Peptide name
Rac GTPase-activating protein 1

Ligandability

Cysteine 300 of Rac GTPase-activating protein 1

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 331 of Rac GTPase-activating protein 1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Rac GTPase-activating protein 1 between cysteines 316 and 331. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
4b6d
Structure name
structure of the atypical c1 domain of mgcracgap
Structure deposition date
2012-08-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
7
% buried
48
Peptide accession
Q9H0H5
Residue number A
316
Residue number B
331
Peptide name
Rac GTPase-activating protein 1

Ligandability

Cysteine 316 of Rac GTPase-activating protein 1

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 331 of Rac GTPase-activating protein 1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Rac GTPase-activating protein 1 between cysteines 16 and 109 (16 and 83 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
5c2k
Structure name
crystal structure of the fusion protein linked by rhoa and the gap domain of mgcracgap
Structure deposition date
2015-06-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
93
Minimum pKa ?
13
% buried
100
Peptide accession
Q9H0H5
Residue number A
16
Residue number B
109
Peptide name
Rac GTPase-activating protein 1

Ligandability

Cysteine 16 of Rac GTPase-activating protein 1

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 109 of Rac GTPase-activating protein 1

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 16 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Rac GTPase-activating protein 1 between cysteines 327 and 331. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4b6d
Structure name
structure of the atypical c1 domain of mgcracgap
Structure deposition date
2012-08-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
82
Peptide accession
Q9H0H5
Residue number A
327
Residue number B
331
Peptide name
Rac GTPase-activating protein 1

Ligandability

Cysteine 327 of Rac GTPase-activating protein 1

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 331 of Rac GTPase-activating protein 1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Rac GTPase-activating protein 1 between cysteines 319 and 331. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
4b6d
Structure name
structure of the atypical c1 domain of mgcracgap
Structure deposition date
2012-08-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
56
Peptide accession
Q9H0H5
Residue number A
319
Residue number B
331
Peptide name
Rac GTPase-activating protein 1

Ligandability

Cysteine 319 of Rac GTPase-activating protein 1

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 331 of Rac GTPase-activating protein 1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Rac GTPase-activating protein 1 between cysteines 303 and 331. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4b6d
Structure name
structure of the atypical c1 domain of mgcracgap
Structure deposition date
2012-08-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
7
% buried
44
Peptide accession
Q9H0H5
Residue number A
303
Residue number B
331
Peptide name
Rac GTPase-activating protein 1

Ligandability

Cysteine 303 of Rac GTPase-activating protein 1

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 331 of Rac GTPase-activating protein 1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Rac GTPase-activating protein 1 between cysteines 331 and 335. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
4b6d
Structure name
structure of the atypical c1 domain of mgcracgap
Structure deposition date
2012-08-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
42
Peptide accession
Q9H0H5
Residue number A
331
Residue number B
335
Peptide name
Rac GTPase-activating protein 1

Ligandability

Cysteine 331 of Rac GTPase-activating protein 1

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 335 of Rac GTPase-activating protein 1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Rac GTPase-activating protein 1 between cysteines 369 and 419. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3wpq
Structure name
crystal structure of the gap domain of mgcracgap(s387a)
Structure deposition date
2014-01-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
98
Peptide accession
Q9H0H5
Residue number A
369
Residue number B
419
Peptide name
Rac GTPase-activating protein 1

Ligandability

Cysteine 369 of Rac GTPase-activating protein 1

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 419 of Rac GTPase-activating protein 1

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 Rac GTPase-activating protein 1 between cysteines 109 and 159 (83 and 159 respectively in this structure).

Details

Redox score ?
nan
PDB code
5c2k
Structure name
crystal structure of the fusion protein linked by rhoa and the gap domain of mgcracgap
Structure deposition date
2015-06-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
100
Peptide accession
Q9H0H5
Residue number A
109
Residue number B
159
Peptide name
Rac GTPase-activating protein 1

Ligandability

Cysteine 109 of Rac GTPase-activating protein 1

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 159 of Rac GTPase-activating protein 1

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 159 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Rac GTPase-activating protein 1 between cysteines 16 and 159.

Details

Redox score ?
nan
PDB code
5c2k
Structure name
crystal structure of the fusion protein linked by rhoa and the gap domain of mgcracgap
Structure deposition date
2015-06-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
100
Peptide accession
Q9H0H5
Residue number A
16
Residue number B
159
Peptide name
Rac GTPase-activating protein 1

Ligandability

Cysteine 16 of Rac GTPase-activating protein 1

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 159 of Rac GTPase-activating protein 1

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 16 in protein A could not be asigned to a Uniprot residue.
Cysteine 159 in protein B could not be asigned to a Uniprot residue.
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