ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Eukaryotic translation initiation factor 3 subunit C

Intramolecular
Cysteine 567 and cysteine 571
Cysteine 401 and cysteine 404
Cysteine 500 and cysteine 552
A redox-regulated disulphide may form within Eukaryotic translation initiation factor 3 subunit C between cysteines 567 and 571.

Details

Redox score ?
66
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)
5
Half-sphere exposure sum ?
81
Minimum pKa ?
8
% buried
92
Peptide accession
G1U971
Residue number A
567
Residue number B
571
Peptide name
Eukaryotic translation initiation factor 3 subunit C

Ligandability

Cysteine 567 of Eukaryotic translation initiation factor 3 subunit C

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 571 of Eukaryotic translation initiation factor 3 subunit C

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 C between cysteines 401 and 404. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
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)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
76
Peptide accession
G1U971
Residue number A
401
Residue number B
404
Peptide name
Eukaryotic translation initiation factor 3 subunit C

Ligandability

Cysteine 401 of Eukaryotic translation initiation factor 3 subunit C

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 404 of Eukaryotic translation initiation factor 3 subunit C

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 C between cysteines 500 and 552. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
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 ?
61
Minimum pKa ?
9
% buried
44
Peptide accession
G1U971
Residue number A
500
Residue number B
552
Peptide name
Eukaryotic translation initiation factor 3 subunit C

Ligandability

Cysteine 500 of Eukaryotic translation initiation factor 3 subunit C

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 552 of Eukaryotic translation initiation factor 3 subunit C

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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