ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Eukaryotic translation initiation factor 4 gamma 3

Intramolecular
Cysteine 813 and cysteine 841
Cysteine 813 and cysteine 815
Cysteine 913 and cysteine 928
Cysteine 841 and cysteine 913
Cysteine 928 and cysteine 930
A redox-regulated disulphide may form within Eukaryotic translation initiation factor 4 gamma 3 between cysteines 813 and 841. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
1hu3
Structure name
middle domain of human eif4gii
Structure deposition date
2001-01-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
12
% buried
94
Peptide accession
O43432
Residue number A
813
Residue number B
841
Peptide name
Eukaryotic translation initiation factor 4 gamma 3

Ligandability

Cysteine 813 of Eukaryotic translation initiation factor 4 gamma 3

Cysteine 841 of Eukaryotic translation initiation factor 4 gamma 3

A redox-regulated disulphide may form within Eukaryotic translation initiation factor 4 gamma 3 between cysteines 813 and 815. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
1hu3
Structure name
middle domain of human eif4gii
Structure deposition date
2001-01-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
11
% buried
68
Peptide accession
O43432
Residue number A
813
Residue number B
815
Peptide name
Eukaryotic translation initiation factor 4 gamma 3

Ligandability

Cysteine 813 of Eukaryotic translation initiation factor 4 gamma 3

Cysteine 815 of Eukaryotic translation initiation factor 4 gamma 3

A redox-regulated disulphide may form within Eukaryotic translation initiation factor 4 gamma 3 between cysteines 913 and 928. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1hu3
Structure name
middle domain of human eif4gii
Structure deposition date
2001-01-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
86
Peptide accession
O43432
Residue number A
913
Residue number B
928
Peptide name
Eukaryotic translation initiation factor 4 gamma 3

Ligandability

Cysteine 913 of Eukaryotic translation initiation factor 4 gamma 3

Cysteine 928 of Eukaryotic translation initiation factor 4 gamma 3

A redox-regulated disulphide may form within Eukaryotic translation initiation factor 4 gamma 3 between cysteines 841 and 913. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1hu3
Structure name
middle domain of human eif4gii
Structure deposition date
2001-01-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
91
Peptide accession
O43432
Residue number A
841
Residue number B
913
Peptide name
Eukaryotic translation initiation factor 4 gamma 3

Ligandability

Cysteine 841 of Eukaryotic translation initiation factor 4 gamma 3

Cysteine 913 of Eukaryotic translation initiation factor 4 gamma 3

A redox-regulated disulphide may form within Eukaryotic translation initiation factor 4 gamma 3 between cysteines 928 and 930. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
1hu3
Structure name
middle domain of human eif4gii
Structure deposition date
2001-01-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
72
Peptide accession
O43432
Residue number A
928
Residue number B
930
Peptide name
Eukaryotic translation initiation factor 4 gamma 3

Ligandability

Cysteine 928 of Eukaryotic translation initiation factor 4 gamma 3

Cysteine 930 of Eukaryotic translation initiation factor 4 gamma 3

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