ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Eukaryotic translation initiation factor 4 gamma 2

Intramolecular
Cysteine 231 and cysteine 253 L
Cysteine 97 and cysteine 136
Cysteine 253 and cysteine 255 L
A redox-regulated disulphide may form within Eukaryotic translation initiation factor 4 gamma 2 between cysteines 231 and 253. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4iul
Structure name
mif4g domain of dap5
Structure deposition date
2013-01-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
92
Peptide accession
P78344
Residue number A
231
Residue number B
253
Peptide name
Eukaryotic translation initiation factor 4 gamma 2

Ligandability

Cysteine 231 of Eukaryotic translation initiation factor 4 gamma 2

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 253 of Eukaryotic translation initiation factor 4 gamma 2

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 Eukaryotic translation initiation factor 4 gamma 2 between cysteines 97 and 136. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4iul
Structure name
mif4g domain of dap5
Structure deposition date
2013-01-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
70
Peptide accession
P78344
Residue number A
97
Residue number B
136
Peptide name
Eukaryotic translation initiation factor 4 gamma 2

Ligandability

Cysteine 97 of Eukaryotic translation initiation factor 4 gamma 2

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 136 of Eukaryotic translation initiation factor 4 gamma 2

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 4 gamma 2 between cysteines 253 and 255. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
4iul
Structure name
mif4g domain of dap5
Structure deposition date
2013-01-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
81
Peptide accession
P78344
Residue number A
253
Residue number B
255
Peptide name
Eukaryotic translation initiation factor 4 gamma 2

Ligandability

Cysteine 253 of Eukaryotic translation initiation factor 4 gamma 2

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.

Cysteine 255 of Eukaryotic translation initiation factor 4 gamma 2

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.

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