ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Histidine--tRNA ligase, cytoplasmic

Intramolecular
Cysteine 191 and cysteine 379
Cysteine 83 and cysteine 196
Cysteine 83 and cysteine 174
A redox-regulated disulphide may form within Histidine--tRNA ligase, cytoplasmic between cysteines 191 and 379. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
4g85
Structure name
crystal structure of human hisrs
Structure deposition date
2012-07-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
87
Minimum pKa ?
13
% buried
100
Peptide accession
P12081
Residue number A
191
Residue number B
379
Peptide name
Histidine--tRNA ligase, cytoplasmic

Ligandability

Cysteine 191 of Histidine--tRNA ligase, cytoplasmic

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 379 of Histidine--tRNA ligase, cytoplasmic

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 Histidine--tRNA ligase, cytoplasmic between cysteines 83 and 196. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
5w6m
Structure name
crystal structure of the human histidyl-trna synthetase mutant d175e
Structure deposition date
2017-06-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
100
Peptide accession
P12081
Residue number A
83
Residue number B
196
Peptide name
Histidine--tRNA ligase, cytoplasmic

Ligandability

Cysteine 83 of Histidine--tRNA ligase, cytoplasmic

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 196 of Histidine--tRNA ligase, cytoplasmic

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 Histidine--tRNA ligase, cytoplasmic between cysteines 83 and 174. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
4g85
Structure name
crystal structure of human hisrs
Structure deposition date
2012-07-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
13
% buried
100
Peptide accession
P12081
Residue number A
83
Residue number B
174
Peptide name
Histidine--tRNA ligase, cytoplasmic

Ligandability

Cysteine 83 of Histidine--tRNA ligase, cytoplasmic

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 174 of Histidine--tRNA ligase, cytoplasmic

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.

If this tool was useful for finding a disulphide, please cite: