ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Rho-related GTP-binding protein RhoB

Intramolecular
Cysteine 16 and cysteine 83
Cysteine 83 and cysteine 159
Cysteine 16 and cysteine 159
A redox-regulated disulphide may form within Rho-related GTP-binding protein RhoB between cysteines 16 and 83. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
6hxu
Structure name
crystal structure of human rhob q63l in complex with gtp
Structure deposition date
2018-10-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
93
Minimum pKa ?
13
% buried
100
Peptide accession
P62745
Residue number A
16
Residue number B
83
Peptide name
Rho-related GTP-binding protein RhoB

Ligandability

Cysteine 16 of Rho-related GTP-binding protein RhoB

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 Rho-related GTP-binding protein RhoB

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 RhoB 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 ?
43
PDB code
6sge
Structure name
crystal structure of human rhob-gtp in complex with nanobody b6
Structure deposition date
2019-08-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
100
Peptide accession
P62745
Residue number A
83
Residue number B
159
Peptide name
Rho-related GTP-binding protein RhoB

Ligandability

Cysteine 83 of Rho-related GTP-binding protein RhoB

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 RhoB

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 RhoB 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 ?
27
PDB code
6hxu
Structure name
crystal structure of human rhob q63l in complex with gtp
Structure deposition date
2018-10-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
100
Peptide accession
P62745
Residue number A
16
Residue number B
159
Peptide name
Rho-related GTP-binding protein RhoB

Ligandability

Cysteine 16 of Rho-related GTP-binding protein RhoB

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 RhoB

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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