ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Arginine--tRNA ligase, cytoplasmic

Intramolecular
Cysteine 617 and cysteine 638
Cysteine 615 and cysteine 617
Cysteine 32 and cysteine 34 L
Cysteine 615 and cysteine 638
A redox-regulated disulphide may form within Arginine--tRNA ligase, cytoplasmic between cysteines 617 and 638 (545 and 566 respectively in this structure).

Details

Redox score ?
72
PDB code
4q2t
Structure name
crystal structure of arginyl-trna synthetase complexed with l-arginine
Structure deposition date
2014-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
8
% buried
86
Peptide accession
P54136
Residue number A
617
Residue number B
638
Peptide name
Arginine--tRNA ligase, cytoplasmic

Ligandability

Cysteine 617 of Arginine--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 638 of Arginine--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 Arginine--tRNA ligase, cytoplasmic between cysteines 615 and 617. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
4r3z
Structure name
crystal structure of human argrs-glnrs-aimp1 complex
Structure deposition date
2014-08-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
44
Peptide accession
P54136
Residue number A
615
Residue number B
617
Peptide name
Arginine--tRNA ligase, cytoplasmic

Ligandability

Cysteine 615 of Arginine--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 617 of Arginine--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 Arginine--tRNA ligase, cytoplasmic between cysteines 32 and 34. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
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 ?
22
Minimum pKa ?
9
% buried
0
Peptide accession
P54136
Residue number A
32
Residue number B
34
Peptide name
Arginine--tRNA ligase, cytoplasmic

Ligandability

Cysteine 32 of Arginine--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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 34 of Arginine--tRNA ligase, cytoplasmic

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

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 Arginine--tRNA ligase, cytoplasmic between cysteines 615 and 638 (543 and 566 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4q2t
Structure name
crystal structure of arginyl-trna synthetase complexed with l-arginine
Structure deposition date
2014-04-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
65
Peptide accession
P54136
Residue number A
615
Residue number B
638
Peptide name
Arginine--tRNA ligase, cytoplasmic

Ligandability

Cysteine 615 of Arginine--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 638 of Arginine--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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