ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Rho-related GTP-binding protein RhoQ

Intramolecular
Cysteine 158 and cysteine 159
Cysteine 87 and cysteine 163
Cysteine 12 and cysteine 87
A redox-regulated disulphide may form within Rho-related GTP-binding protein RhoQ between cysteines 158 and 159 (166 and 167 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
2atx
Structure name
crystal structure of the tc10 gppnhp complex
Structure deposition date
2005-08-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
36
Peptide accession
P17081
Residue number A
158
Residue number B
159
Peptide name
Rho-related GTP-binding protein RhoQ

Ligandability

Cysteine 158 of Rho-related GTP-binding protein RhoQ

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 Rho-related GTP-binding protein RhoQ

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 Rho-related GTP-binding protein RhoQ between cysteines 87 and 163 (95 and 171 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
2atx
Structure name
crystal structure of the tc10 gppnhp complex
Structure deposition date
2005-08-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
100
Peptide accession
P17081
Residue number A
87
Residue number B
163
Peptide name
Rho-related GTP-binding protein RhoQ

Ligandability

Cysteine 87 of Rho-related GTP-binding protein RhoQ

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 163 of Rho-related GTP-binding protein RhoQ

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 Rho-related GTP-binding protein RhoQ between cysteines 12 and 87 (20 and 95 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
2atx
Structure name
crystal structure of the tc10 gppnhp complex
Structure deposition date
2005-08-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
12
% buried
100
Peptide accession
P17081
Residue number A
12
Residue number B
87
Peptide name
Rho-related GTP-binding protein RhoQ

Ligandability

Cysteine 12 of Rho-related GTP-binding protein RhoQ

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 87 of Rho-related GTP-binding protein RhoQ

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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