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Crystal structure of the editing domain of E. COLI leucyl-tRNA synthetase

Analyse Crystal structure of the editing domain of E. COLI leucyl-tRNA synthetase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2AJG
Type
protein
Length
360 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Leucyl-tRNA synthetase
EC
6.1.1.4
UniProt
P07813
Pockets
5 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALeucyl-tRNA synthetase (EC 6.1.1.4)protein18631% helix, 24% strandP07813
BLeucyl-tRNA synthetase (EC 6.1.1.4)protein17430% helix, 24% strandP07813

Pockets

5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13820.690.8135empty
21610.460.7622empty
31060.440.7828empty
4630.300.7414empty
5590.270.7313empty

Interfaces

1 interface between chains.

  • A–B · 549 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 2AJG · Crystal structure of the editing domain of E. coli leucyl-tRNA synthetase · the same entry in another collection · chain A against A, TM-score 1.00
  • P07813 · AlphaFold monomer V2.0 prediction for leucine--tRNA ligase (P07813) · a predicted model of the same protein · chain B against A, TM-score 0.98

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