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Crystal structure of a truncated human cytosolic methionyl-tRNA synthetase

Analyse Crystal structure of a truncated human cytosolic methionyl-tRNA synthetase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5GL7
Type
protein
Length
597 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Methionine--tRNA ligase, cytoplasmic
EC
6.1.1.10
UniProt
P56192
Ligands
ZN
Pockets
6 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMethionine--tRNA ligase, cytoplasmic (EC 6.1.1.10)protein59748% helix, 15% strandP56192

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A
  • GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13660.610.7754empty
21990.480.7624GOL
32070.460.7429empty
4610.340.7817empty
5560.270.7315empty

Compared structures

  • 5GL7 · Crystal structure of a truncated human cytosolic methionyl-tRNA synthetase · the same entry in another collection · chain A against A, TM-score 1.00
  • P56192 · AlphaFold monomer V2.0 prediction for methionine--tRNA ligase, cytoplasmic (P56192) · a predicted model of the same protein · chain A against A, TM-score 0.99

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