ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Eukaryotic translation initiation factor 3 subunit M

Intramolecular
Cysteine 49 and cysteine 52
Cysteine 52 and cysteine 87
Cysteine 87 and cysteine 125
A redox-regulated disulphide may form within Eukaryotic translation initiation factor 3 subunit M between cysteines 49 and 52.

Details

Redox score ?
60
PDB code
5a5t
Structure name
structure of mammalian eif3 in the context of the 43s preinitiation complex
Structure deposition date
2015-06-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
50
Minimum pKa ?
10
% buried
36
Peptide accession
G1SLW8
Residue number A
49
Residue number B
52
Peptide name
Eukaryotic translation initiation factor 3 subunit M

Ligandability

Cysteine 49 of Eukaryotic translation initiation factor 3 subunit M

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 52 of Eukaryotic translation initiation factor 3 subunit M

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 M between cysteines 52 and 87. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
5a5t
Structure name
structure of mammalian eif3 in the context of the 43s preinitiation complex
Structure deposition date
2015-06-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
69
Peptide accession
G1SLW8
Residue number A
52
Residue number B
87
Peptide name
Eukaryotic translation initiation factor 3 subunit M

Ligandability

Cysteine 52 of Eukaryotic translation initiation factor 3 subunit M

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 87 of Eukaryotic translation initiation factor 3 subunit M

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 M between cysteines 87 and 125. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5a5t
Structure name
structure of mammalian eif3 in the context of the 43s preinitiation complex
Structure deposition date
2015-06-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
64
Peptide accession
G1SLW8
Residue number A
87
Residue number B
125
Peptide name
Eukaryotic translation initiation factor 3 subunit M

Ligandability

Cysteine 87 of Eukaryotic translation initiation factor 3 subunit M

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 125 of Eukaryotic translation initiation factor 3 subunit M

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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