ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Lysine--tRNA ligase

Intramolecular
Cysteine 427 and cysteine 434 L
Cysteine 456 and cysteine 463
Cysteine 338 and cysteine 496
A redox-regulated disulphide may form within Lysine--tRNA ligase between cysteines 427 and 434.

Details

Redox score ?
67
PDB code
7ea9
Structure name
crystal structure of human lysyl-trna synthetase y145h mutant
Structure deposition date
2021-03-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
31
Peptide accession
Q15046
Residue number A
427
Residue number B
434
Peptide name
Lysine--tRNA ligase

Ligandability

Cysteine 427 of Lysine--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 434 of Lysine--tRNA ligase

Not ligandable in the dataset of Yang et al.

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 Lysine--tRNA ligase between cysteines 456 and 463. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6ild
Structure name
crystal structure of human lysrs: p38/aimp2 complex ii
Structure deposition date
2018-10-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
82
Peptide accession
Q15046
Residue number A
456
Residue number B
463
Peptide name
Lysine--tRNA ligase

Ligandability

Cysteine 456 of Lysine--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 463 of Lysine--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 Lysine--tRNA ligase between cysteines 338 and 496. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
4dpg
Structure name
crystal structure of human lysrs: p38/aimp2 complex i
Structure deposition date
2012-02-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
100
Peptide accession
Q15046
Residue number A
338
Residue number B
496
Peptide name
Lysine--tRNA ligase

Ligandability

Cysteine 338 of Lysine--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 496 of Lysine--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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