ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Negative elongation factor C/D

Intramolecular
Cysteine 397 and cysteine 398 L
Cysteine 397 and cysteine 417 L
Cysteine 195 and cysteine 232 L
A redox-regulated disulphide may form within Negative elongation factor C/D between cysteines 397 and 398. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
5l3x
Structure name
crystal structure of negative elongation factor subcomplex nelf-ac
Structure deposition date
2016-05-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
71
Peptide accession
Q8IXH7
Residue number A
397
Residue number B
398
Peptide name
Negative elongation factor C/D

Ligandability

Cysteine 397 of Negative elongation factor C/D

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 398 of Negative elongation factor C/D

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Negative elongation factor C/D between cysteines 397 and 417. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
5l3x
Structure name
crystal structure of negative elongation factor subcomplex nelf-ac
Structure deposition date
2016-05-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
71
Peptide accession
Q8IXH7
Residue number A
397
Residue number B
417
Peptide name
Negative elongation factor C/D

Ligandability

Cysteine 397 of Negative elongation factor C/D

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 417 of Negative elongation factor C/D

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 Negative elongation factor C/D between cysteines 195 and 232. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
5l3x
Structure name
crystal structure of negative elongation factor subcomplex nelf-ac
Structure deposition date
2016-05-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
72
Peptide accession
Q8IXH7
Residue number A
195
Residue number B
232
Peptide name
Negative elongation factor C/D

Ligandability

Cysteine 195 of Negative elongation factor C/D

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.

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 232 of Negative elongation factor C/D

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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