ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Eukaryotic translation initiation factor 2A

Intramolecular
Cysteine 39 and cysteine 42
Cysteine 132 and cysteine 142
Cysteine 80 and cysteine 132
A redox-regulated disulphide may form within Eukaryotic translation initiation factor 2A between cysteines 39 and 42.

Details

Redox score ?
68
PDB code
8dys
Structure name
crystal structure of human eukaryotic translation initiation factor 2a (eif2a)
Structure deposition date
2022-08-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BY44
Residue number A
39
Residue number B
42
Peptide name
Eukaryotic translation initiation factor 2A

Ligandability

Cysteine 39 of Eukaryotic translation initiation factor 2A

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 42 of Eukaryotic translation initiation factor 2A

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 2A between cysteines 132 and 142. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
8dys
Structure name
crystal structure of human eukaryotic translation initiation factor 2a (eif2a)
Structure deposition date
2022-08-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BY44
Residue number A
132
Residue number B
142
Peptide name
Eukaryotic translation initiation factor 2A

Ligandability

Cysteine 132 of Eukaryotic translation initiation factor 2A

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 142 of Eukaryotic translation initiation factor 2A

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 2A between cysteines 80 and 132. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
8dys
Structure name
crystal structure of human eukaryotic translation initiation factor 2a (eif2a)
Structure deposition date
2022-08-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BY44
Residue number A
80
Residue number B
132
Peptide name
Eukaryotic translation initiation factor 2A

Ligandability

Cysteine 80 of Eukaryotic translation initiation factor 2A

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 132 of Eukaryotic translation initiation factor 2A

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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