ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Translation initiation factor eIF-2B subunit epsilon

Intramolecular
Cysteine 372 and cysteine 383
Cysteine 95 and cysteine 96
Cysteine 95 and cysteine 112
A redox-regulated disulphide may form within Translation initiation factor eIF-2B subunit epsilon between cysteines 372 and 383. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6k71
Structure name
eif2 - eif2b complex
Structure deposition date
2019-06-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
69
Peptide accession
Q13144
Residue number A
372
Residue number B
383
Peptide name
Translation initiation factor eIF-2B subunit epsilon

Ligandability

Cysteine 372 of Translation initiation factor eIF-2B subunit epsilon

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 383 of Translation initiation factor eIF-2B subunit epsilon

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 Translation initiation factor eIF-2B subunit epsilon between cysteines 95 and 96. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7d44
Structure name
eif2b-eif2(ap), ap2 complex
Structure deposition date
2020-09-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
64
Peptide accession
Q13144
Residue number A
95
Residue number B
96
Peptide name
Translation initiation factor eIF-2B subunit epsilon

Ligandability

Cysteine 95 of Translation initiation factor eIF-2B subunit epsilon

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 96 of Translation initiation factor eIF-2B subunit epsilon

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 Translation initiation factor eIF-2B subunit epsilon between cysteines 95 and 112. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
7d44
Structure name
eif2b-eif2(ap), ap2 complex
Structure deposition date
2020-09-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
70
Peptide accession
Q13144
Residue number A
95
Residue number B
112
Peptide name
Translation initiation factor eIF-2B subunit epsilon

Ligandability

Cysteine 95 of Translation initiation factor eIF-2B subunit epsilon

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 112 of Translation initiation factor eIF-2B subunit epsilon

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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