ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Asparagine--tRNA ligase, cytoplasmic

Intramolecular
Cysteine 165 and cysteine 167
Cysteine 158 and cysteine 202
Cysteine 167 and cysteine 202
Cysteine 165 and cysteine 202
Cysteine 438 and cysteine 452
Cysteine 307 and cysteine 316
A redox-regulated disulphide may form within Asparagine--tRNA ligase, cytoplasmic between cysteines 165 and 167. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
5xix
Structure name
the canonical domain of human asparaginyl-trna synthetase
Structure deposition date
2017-04-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
13
Peptide accession
O43776
Residue number A
165
Residue number B
167
Peptide name
Asparagine--tRNA ligase, cytoplasmic

Ligandability

Cysteine 165 of Asparagine--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 167 of Asparagine--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 Asparagine--tRNA ligase, cytoplasmic between cysteines 158 and 202. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
5xix
Structure name
the canonical domain of human asparaginyl-trna synthetase
Structure deposition date
2017-04-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
87
Peptide accession
O43776
Residue number A
158
Residue number B
202
Peptide name
Asparagine--tRNA ligase, cytoplasmic

Ligandability

Cysteine 158 of Asparagine--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 202 of Asparagine--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 Asparagine--tRNA ligase, cytoplasmic between cysteines 167 and 202. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
5xix
Structure name
the canonical domain of human asparaginyl-trna synthetase
Structure deposition date
2017-04-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
46
Peptide accession
O43776
Residue number A
167
Residue number B
202
Peptide name
Asparagine--tRNA ligase, cytoplasmic

Ligandability

Cysteine 167 of Asparagine--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 202 of Asparagine--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 Asparagine--tRNA ligase, cytoplasmic between cysteines 165 and 202. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5xix
Structure name
the canonical domain of human asparaginyl-trna synthetase
Structure deposition date
2017-04-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
42
Peptide accession
O43776
Residue number A
165
Residue number B
202
Peptide name
Asparagine--tRNA ligase, cytoplasmic

Ligandability

Cysteine 165 of Asparagine--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 202 of Asparagine--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 Asparagine--tRNA ligase, cytoplasmic between cysteines 438 and 452. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5xix
Structure name
the canonical domain of human asparaginyl-trna synthetase
Structure deposition date
2017-04-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
12
% buried
68
Peptide accession
O43776
Residue number A
438
Residue number B
452
Peptide name
Asparagine--tRNA ligase, cytoplasmic

Ligandability

Cysteine 438 of Asparagine--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 452 of Asparagine--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 Asparagine--tRNA ligase, cytoplasmic between cysteines 307 and 316. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
5xix
Structure name
the canonical domain of human asparaginyl-trna synthetase
Structure deposition date
2017-04-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide accession
O43776
Residue number A
307
Residue number B
316
Peptide name
Asparagine--tRNA ligase, cytoplasmic

Ligandability

Cysteine 307 of Asparagine--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 316 of Asparagine--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.

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