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Crystal structure of the P.KNOWLESI cytosolic leucyl-tRNA synthetase editing domain

Analyse Crystal structure of the P.KNOWLESI 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
5FOF
Type
protein
Length
1,193 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Leucyl-tRNA synthetase
EC
6.1.1.4
UniProt
B3L7I1
Pockets
14 · best druggability 0.73

Structure

x-ray diffraction · 3 distinct chains · 34% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DLeucyl-tRNA synthetase (EC 6.1.1.4)protein30236% helix, 23% strandB3L7I1
BLeucyl-tRNA synthetase (EC 6.1.1.4)protein29034% helix, 22% strandB3L7I1
CLeucyl-tRNA synthetase (EC 6.1.1.4)protein29933% helix, 22% strandB3L7I1

Pockets

14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11320.730.9234empty
21110.700.9231empty
31170.690.9129empty
41070.690.9230empty
58320.680.7585empty

Interfaces

5 interfaces between chains.

  • B–D · 510 Ų buried · 9 hydrogen bonds · protein-protein
  • A–D · 259 Ų buried · 1 hydrogen bond · protein-protein
  • B–C · 198 Ų buried · 3 hydrogen bonds · protein-protein
  • A–B · 196 Ų buried · 0 hydrogen bonds · protein-protein
  • C–D · 39 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

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

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