ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Transforming protein RhoA

Intermolecular
Cysteine 117 of Rap1 GTPase-GDP dissociation stimulator 1 and cysteine 190 L
Intramolecular
Cysteine 16 and cysteine 83
Cysteine 83 and cysteine 159 L
Cysteine 16 and cysteine 20
Cysteine 16 and cysteine 159 L
Cysteine 20 and cysteine 159 L
Cysteine 20 and cysteine 83
A redox-regulated disulphide may form between cysteine 117 of Rap1 GTPase-GDP dissociation stimulator 1 and cysteine 190 of Transforming protein RhoA. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
5zhx
Structure name
crystal structure of smggds-558 and farnesylated rhoa complex
Structure deposition date
2018-03-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
81
Peptide A name
Rap1 GTPase-GDP dissociation stimulator 1
Peptide B name
Transforming protein RhoA
Peptide A accession
P52306
Peptide B accession
P61586
Peptide A residue number
117
Peptide B residue number
190

Ligandability

Cysteine 117 of Rap1 GTPase-GDP dissociation stimulator 1

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 190 of Transforming protein RhoA

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 Transforming protein RhoA between cysteines 16 and 83.

Details

Redox score ?
69
PDB code
1x86
Structure name
crystal structure of the dh/ph domains of leukemia-associated rhogef in complex with rhoa
Structure deposition date
2004-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
7
% buried
99
Peptide accession
P61586
Residue number A
16
Residue number B
83
Peptide name
Transforming protein RhoA

Ligandability

Cysteine 16 of Transforming protein RhoA

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 83 of Transforming protein RhoA

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 Transforming protein RhoA between cysteines 83 and 159. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3tvd
Structure name
crystal structure of mouse rhoa-gtp complex
Structure deposition date
2011-09-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
100
Peptide accession
P61589
Residue number A
83
Residue number B
159
Peptide name
Transforming protein RhoA

Ligandability

Cysteine 83 of Transforming protein RhoA

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 Transforming protein RhoA

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 Transforming protein RhoA between cysteines 16 and 20. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4xh9
Structure name
crystal structure of human rhoa in complex with dh/ph fragment of the guanine nucleotide exchange factor net1
Structure deposition date
2015-01-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
8
% buried
82
Peptide accession
P61586
Residue number A
16
Residue number B
20
Peptide name
Transforming protein RhoA

Ligandability

Cysteine 16 of Transforming protein RhoA

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 20 of Transforming protein RhoA

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 Transforming protein RhoA between cysteines 16 and 159. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3tvd
Structure name
crystal structure of mouse rhoa-gtp complex
Structure deposition date
2011-09-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
100
Peptide accession
P61589
Residue number A
16
Residue number B
159
Peptide name
Transforming protein RhoA

Ligandability

Cysteine 16 of Transforming protein RhoA

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 Transforming protein RhoA

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 Transforming protein RhoA between cysteines 20 and 159. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
1x86
Structure name
crystal structure of the dh/ph domains of leukemia-associated rhogef in complex with rhoa
Structure deposition date
2004-08-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
81
Peptide accession
P61586
Residue number A
20
Residue number B
159
Peptide name
Transforming protein RhoA

Ligandability

Cysteine 20 of Transforming protein RhoA

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 Transforming protein RhoA

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 Transforming protein RhoA between cysteines 20 and 83. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
4xh9
Structure name
crystal structure of human rhoa in complex with dh/ph fragment of the guanine nucleotide exchange factor net1
Structure deposition date
2015-01-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
10
% buried
84
Peptide accession
P61586
Residue number A
20
Residue number B
83
Peptide name
Transforming protein RhoA

Ligandability

Cysteine 20 of Transforming protein RhoA

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 83 of Transforming protein RhoA

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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