ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Eukaryotic translation initiation factor 3 subunit I

Intramolecular
Cysteine 120 and cysteine 144
Cysteine 57 and cysteine 99
Cysteine 76 and cysteine 99
A redox-regulated disulphide may form within Eukaryotic translation initiation factor 3 subunit I between cysteines 120 and 144.

Details

Redox score ?
84
PDB code
5k0y
Structure name
m48s late-stage initiation complex, purified from rabbit reticulocytes lysates, displaying eif2 ternary complex and eif3 i and g subunits relocated to the intersubunit face
Structure deposition date
2016-05-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5IH81
Residue number A
120
Residue number B
144
Peptide name
Eukaryotic translation initiation factor 3 subunit I

Ligandability

Cysteine 120 of Eukaryotic translation initiation factor 3 subunit I

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 144 of Eukaryotic translation initiation factor 3 subunit I

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 I between cysteines 57 and 99.

Details

Redox score ?
63
PDB code
5k0y
Structure name
m48s late-stage initiation complex, purified from rabbit reticulocytes lysates, displaying eif2 ternary complex and eif3 i and g subunits relocated to the intersubunit face
Structure deposition date
2016-05-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
82
Minimum pKa ?
8
% buried
100
Peptide accession
Q5IH81
Residue number A
57
Residue number B
99
Peptide name
Eukaryotic translation initiation factor 3 subunit I

Ligandability

Cysteine 57 of Eukaryotic translation initiation factor 3 subunit I

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 99 of Eukaryotic translation initiation factor 3 subunit I

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 I between cysteines 76 and 99. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
5k0y
Structure name
m48s late-stage initiation complex, purified from rabbit reticulocytes lysates, displaying eif2 ternary complex and eif3 i and g subunits relocated to the intersubunit face
Structure deposition date
2016-05-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
100
Peptide accession
Q5IH81
Residue number A
76
Residue number B
99
Peptide name
Eukaryotic translation initiation factor 3 subunit I

Ligandability

Cysteine 76 of Eukaryotic translation initiation factor 3 subunit I

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 99 of Eukaryotic translation initiation factor 3 subunit I

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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