ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

GTP-binding protein GEM

Intermolecular
Cysteine 215 and cysteine 106
Cysteine 209 and cysteine 106
Intramolecular
Cysteine 209 and cysteine 215
A redox-regulated disulphide may form between two units of GTP-binding protein GEM at cysteines 215 and 106. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2ht6
Structure name
crystal structure of human gem g-domain bound to gdp
Structure deposition date
2006-07-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
73
Peptide A name
GTP-binding protein GEM
Peptide B name
GTP-binding protein GEM
Peptide A accession
P55040
Peptide B accession
P55040
Peptide A residue number
215
Peptide B residue number
106

Ligandability

Cysteine 215 of GTP-binding protein GEM

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 106 of GTP-binding protein GEM

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 between two units of GTP-binding protein GEM at cysteines 209 and 106. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
2ht6
Structure name
crystal structure of human gem g-domain bound to gdp
Structure deposition date
2006-07-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
11
% buried
60
Peptide A name
GTP-binding protein GEM
Peptide B name
GTP-binding protein GEM
Peptide A accession
P55040
Peptide B accession
P55040
Peptide A residue number
209
Peptide B residue number
106

Ligandability

Cysteine 209 of GTP-binding protein GEM

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 106 of GTP-binding protein GEM

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 GTP-binding protein GEM between cysteines 209 and 215. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2g3y
Structure name
crystal structure of the human small gtpase gem
Structure deposition date
2006-02-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
52
Peptide accession
P55040
Residue number A
209
Residue number B
215
Peptide name
GTP-binding protein GEM

Ligandability

Cysteine 209 of GTP-binding protein GEM

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 215 of GTP-binding protein GEM

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.

If this tool was useful for finding a disulphide, please cite: