ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Glutamine--tRNA ligase

Intramolecular
Cysteine 471 and cysteine 478
Cysteine 443 and cysteine 471
Cysteine 443 and cysteine 478
Cysteine 536 and cysteine 556
Cysteine 443 and cysteine 445
Cysteine 443 and cysteine 456
A redox-regulated disulphide may form within Glutamine--tRNA ligase between cysteines 471 and 478.

Details

Redox score ?
71
PDB code
4r3z
Structure name
crystal structure of human argrs-glnrs-aimp1 complex
Structure deposition date
2014-08-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
78
Minimum pKa ?
6
% buried
92
Peptide accession
P47897
Residue number A
471
Residue number B
478
Peptide name
Glutamine--tRNA ligase

Ligandability

Cysteine 471 of Glutamine--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 478 of Glutamine--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 Glutamine--tRNA ligase between cysteines 443 and 471.

Details

Redox score ?
67
PDB code
4r3z
Structure name
crystal structure of human argrs-glnrs-aimp1 complex
Structure deposition date
2014-08-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
9
% buried
100
Peptide accession
P47897
Residue number A
443
Residue number B
471
Peptide name
Glutamine--tRNA ligase

Ligandability

Cysteine 443 of Glutamine--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 471 of Glutamine--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 Glutamine--tRNA ligase between cysteines 443 and 478. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4r3z
Structure name
crystal structure of human argrs-glnrs-aimp1 complex
Structure deposition date
2014-08-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
6
% buried
92
Peptide accession
P47897
Residue number A
443
Residue number B
478
Peptide name
Glutamine--tRNA ligase

Ligandability

Cysteine 443 of Glutamine--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 478 of Glutamine--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 Glutamine--tRNA ligase between cysteines 536 and 556. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
4r3z
Structure name
crystal structure of human argrs-glnrs-aimp1 complex
Structure deposition date
2014-08-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
74
Peptide accession
P47897
Residue number A
536
Residue number B
556
Peptide name
Glutamine--tRNA ligase

Ligandability

Cysteine 536 of Glutamine--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 556 of Glutamine--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 Glutamine--tRNA ligase between cysteines 443 and 445. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
4r3z
Structure name
crystal structure of human argrs-glnrs-aimp1 complex
Structure deposition date
2014-08-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
9
% buried
100
Peptide accession
P47897
Residue number A
443
Residue number B
445
Peptide name
Glutamine--tRNA ligase

Ligandability

Cysteine 443 of Glutamine--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 445 of Glutamine--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 Glutamine--tRNA ligase between cysteines 443 and 456. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4r3z
Structure name
crystal structure of human argrs-glnrs-aimp1 complex
Structure deposition date
2014-08-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
9
% buried
96
Peptide accession
P47897
Residue number A
443
Residue number B
456
Peptide name
Glutamine--tRNA ligase

Ligandability

Cysteine 443 of Glutamine--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 456 of Glutamine--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.

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