ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Eukaryotic translation initiation factor 3 subunit G

Intramolecular
Cysteine 157 and cysteine 169
Cysteine 157 and cysteine 160
Cysteine 160 and cysteine 169
A redox-regulated disulphide may form within Eukaryotic translation initiation factor 3 subunit G between cysteines 157 and 169 (13 and 25 respectively in this structure).

Details

Redox score ?
94
PDB code
2mjc
Structure name
zn-binding domain of eukaryotic translation initiation factor 3, subunit g
Structure deposition date
2014-01-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
5
% buried
0
Peptide accession
O75821
Residue number A
157
Residue number B
169
Peptide name
Eukaryotic translation initiation factor 3 subunit G

Ligandability

Cysteine 157 of Eukaryotic translation initiation factor 3 subunit G

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 169 of Eukaryotic translation initiation factor 3 subunit G

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 Eukaryotic translation initiation factor 3 subunit G between cysteines 157 and 160 (13 and 16 respectively in this structure).

Details

Redox score ?
88
PDB code
2mjc
Structure name
zn-binding domain of eukaryotic translation initiation factor 3, subunit g
Structure deposition date
2014-01-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
5
% buried
0
Peptide accession
O75821
Residue number A
157
Residue number B
160
Peptide name
Eukaryotic translation initiation factor 3 subunit G

Ligandability

Cysteine 157 of Eukaryotic translation initiation factor 3 subunit G

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 160 of Eukaryotic translation initiation factor 3 subunit G

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 Eukaryotic translation initiation factor 3 subunit G between cysteines 160 and 169 (16 and 25 respectively in this structure).

Details

Redox score ?
80
PDB code
2mjc
Structure name
zn-binding domain of eukaryotic translation initiation factor 3, subunit g
Structure deposition date
2014-01-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
9
% buried
0
Peptide accession
O75821
Residue number A
160
Residue number B
169
Peptide name
Eukaryotic translation initiation factor 3 subunit G

Ligandability

Cysteine 160 of Eukaryotic translation initiation factor 3 subunit G

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 169 of Eukaryotic translation initiation factor 3 subunit G

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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