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Crystal structure of the P.FALCIPARUM cytosolic leucyl-tRNA synthetase editing domain (space group P1) containing deletions of insertions 1 and 3

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

PDB
5FOD
Type
protein
Length
619 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
C6KT64
Pockets
5 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALeucyl-tRNA synthetase (EC 6.1.1.4)protein30339% helix, 22% strandC6KT64
BLeucyl-tRNA synthetase (EC 6.1.1.4)protein31638% helix, 21% strandC6KT64

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17570.770.8160empty
23630.730.8536EDO
3720.400.7916empty
4790.400.7819empty
5730.340.7620empty

Interfaces

1 interface between chains.

  • A–B · 637 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 5FOD · Crystal structure of the P.falciparum cytosolic leucyl-tRNA synthetase editing domain… · the same entry in another collection · chain A against A, TM-score 1.00

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