ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Bifunctional glutamate/proline--tRNA ligase

Intermolecular
Cysteine 105 and cysteine 205 of Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
Intramolecular
Cysteine 1495 and cysteine 1497
Cysteine 1453 and cysteine 1480
Cysteine 1448 and cysteine 1495
Cysteine 1453 and cysteine 1497
Cysteine 1495 and cysteine 1480
Cysteine 1453 and cysteine 1495
Cysteine 1448 and cysteine 1497
Cysteine 1448 and cysteine 1480
Cysteine 1448 and cysteine 1453
More...
Cysteine 1309 and cysteine 1327
Cysteine 1076 and cysteine 1148 L
A redox-regulated disulphide may form between cysteine 105 of Bifunctional glutamate/proline--tRNA ligase and cysteine 205 of Aminoacyl tRNA synthase complex-interacting multifunctional protein 2.

Details

Redox score ?
78
PDB code
5a34
Structure name
the crystal structure of the gst-like domains complex of eprs-aimp2
Structure deposition date
2015-05-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
88
Peptide A name
Bifunctional glutamate/proline--tRNA ligase
Peptide B name
Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
Peptide A accession
P07814
Peptide B accession
Q13155
Peptide A residue number
105
Peptide B residue number
205

Ligandability

Cysteine 105 of Bifunctional glutamate/proline--tRNA ligase

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 205 of Aminoacyl tRNA synthase complex-interacting multifunctional protein 2

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 Bifunctional glutamate/proline--tRNA ligase between cysteines 1495 and 1497.

Details

Redox score ?
89
PDB code
7f9d
Structure name
homo sapiens prolyl-trna synthetase (hsprs) in complex with l-proline and compound l96
Structure deposition date
2021-07-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
4
% buried
34
Peptide accession
P07814
Residue number A
1495
Residue number B
1497
Peptide name
Bifunctional glutamate/proline--tRNA ligase

Ligandability

Cysteine 1495 of Bifunctional glutamate/proline--tRNA ligase

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 1497 of Bifunctional glutamate/proline--tRNA ligase

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 Bifunctional glutamate/proline--tRNA ligase between cysteines 1453 and 1480 (1453 and 1497 respectively in this structure).

Details

Redox score ?
87
PDB code
5vad
Structure name
crystal structure of human prolyl-trna synthetase (prs) in complex with inhibitor
Structure deposition date
2017-03-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
nan
Minimum pKa ?
8
% buried
18
Peptide accession
P07814
Residue number A
1453
Residue number B
1480
Peptide name
Bifunctional glutamate/proline--tRNA ligase

Ligandability

Cysteine 1453 of Bifunctional glutamate/proline--tRNA ligase

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 1480 of Bifunctional glutamate/proline--tRNA ligase

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 Bifunctional glutamate/proline--tRNA ligase between cysteines 1448 and 1495.

Details

Redox score ?
84
PDB code
7f9a
Structure name
homo sapiens prolyl-trna synthetase (hsprs) in complex with l-proline and compound l97
Structure deposition date
2021-07-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
4
% buried
41
Peptide accession
P07814
Residue number A
1448
Residue number B
1495
Peptide name
Bifunctional glutamate/proline--tRNA ligase

Ligandability

Cysteine 1448 of Bifunctional glutamate/proline--tRNA ligase

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 1495 of Bifunctional glutamate/proline--tRNA ligase

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 Bifunctional glutamate/proline--tRNA ligase between cysteines 1453 and 1497.

Details

Redox score ?
78
PDB code
7ot0
Structure name
human prolyl-trna synthetase in complex with l-proline and compound 4h
Structure deposition date
2021-06-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
32
Peptide accession
P07814
Residue number A
1453
Residue number B
1497
Peptide name
Bifunctional glutamate/proline--tRNA ligase

Ligandability

Cysteine 1453 of Bifunctional glutamate/proline--tRNA ligase

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 1497 of Bifunctional glutamate/proline--tRNA ligase

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 Bifunctional glutamate/proline--tRNA ligase between cysteines 1495 and 1480 (1495 and 1497 respectively in this structure).

Details

Redox score ?
78
PDB code
5vad
Structure name
crystal structure of human prolyl-trna synthetase (prs) in complex with inhibitor
Structure deposition date
2017-03-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
8
% buried
27
Peptide accession
P07814
Residue number A
1495
Residue number B
1480
Peptide name
Bifunctional glutamate/proline--tRNA ligase

Ligandability

Cysteine 1495 of Bifunctional glutamate/proline--tRNA ligase

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 1480 of Bifunctional glutamate/proline--tRNA ligase

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 Bifunctional glutamate/proline--tRNA ligase between cysteines 1453 and 1495.

Details

Redox score ?
76
PDB code
7ot3
Structure name
human prolyl-trna synthetase in complex with l-proline and compound 3b
Structure deposition date
2021-06-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
38
Peptide accession
P07814
Residue number A
1453
Residue number B
1495
Peptide name
Bifunctional glutamate/proline--tRNA ligase

Ligandability

Cysteine 1453 of Bifunctional glutamate/proline--tRNA ligase

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 1495 of Bifunctional glutamate/proline--tRNA ligase

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 Bifunctional glutamate/proline--tRNA ligase between cysteines 1448 and 1497.

Details

Redox score ?
76
PDB code
7f9d
Structure name
homo sapiens prolyl-trna synthetase (hsprs) in complex with l-proline and compound l96
Structure deposition date
2021-07-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
23
Peptide accession
P07814
Residue number A
1448
Residue number B
1497
Peptide name
Bifunctional glutamate/proline--tRNA ligase

Ligandability

Cysteine 1448 of Bifunctional glutamate/proline--tRNA ligase

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 1497 of Bifunctional glutamate/proline--tRNA ligase

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 Bifunctional glutamate/proline--tRNA ligase between cysteines 1448 and 1480 (1448 and 1497 respectively in this structure).

Details

Redox score ?
74
PDB code
5vad
Structure name
crystal structure of human prolyl-trna synthetase (prs) in complex with inhibitor
Structure deposition date
2017-03-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
8
% buried
16
Peptide accession
P07814
Residue number A
1448
Residue number B
1480
Peptide name
Bifunctional glutamate/proline--tRNA ligase

Ligandability

Cysteine 1448 of Bifunctional glutamate/proline--tRNA ligase

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 1480 of Bifunctional glutamate/proline--tRNA ligase

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 Bifunctional glutamate/proline--tRNA ligase between cysteines 1448 and 1453.

Details

Redox score ?
73
PDB code
7f9c
Structure name
homo sapiens prolyl-trna synthetase (hsprs) in complex with l-proline and compound l96
Structure deposition date
2021-07-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
42
Peptide accession
P07814
Residue number A
1448
Residue number B
1453
Peptide name
Bifunctional glutamate/proline--tRNA ligase

Ligandability

Cysteine 1448 of Bifunctional glutamate/proline--tRNA ligase

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 1453 of Bifunctional glutamate/proline--tRNA ligase

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 Bifunctional glutamate/proline--tRNA ligase between cysteines 1309 and 1327 (309 and 327 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4k88
Structure name
crystal structure of human prolyl-trna synthetase (halofuginone bound form)
Structure deposition date
2013-04-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
70
Peptide accession
P07814
Residue number A
1309
Residue number B
1327
Peptide name
Bifunctional glutamate/proline--tRNA ligase

Ligandability

Cysteine 1309 of Bifunctional glutamate/proline--tRNA ligase

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 1327 of Bifunctional glutamate/proline--tRNA ligase

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 Bifunctional glutamate/proline--tRNA ligase between cysteines 1076 and 1148. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
7ot3
Structure name
human prolyl-trna synthetase in complex with l-proline and compound 3b
Structure deposition date
2021-06-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
12
% buried
100
Peptide accession
P07814
Residue number A
1076
Residue number B
1148
Peptide name
Bifunctional glutamate/proline--tRNA ligase

Ligandability

Cysteine 1076 of Bifunctional glutamate/proline--tRNA ligase

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 1148 of Bifunctional glutamate/proline--tRNA ligase

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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