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Crystal structure of human glycyl-tRNA synthetase (glyrs) in complex with ampcpp

Analyse Crystal structure of human glycyl-tRNA synthetase (glyrs) in complex with ampcpp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ZT6
Type
protein
Length
530 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycyl-tRNA synthetase
EC
6.1.1.14
UniProt
P41250
Ligands
APC
Pockets
6 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlycyl-tRNA synthetase (EC 6.1.1.14)protein53038% helix, 24% strandP41250

Ligands and binding sites

  • APC · Diphosphomethylphosphonic acid adenosyl ester · ligand · 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
111460.810.8283APC
2810.470.8118empty
3520.400.8216empty
41000.380.7526empty
5630.310.7514empty

Compared structures

  • 2ZT6 · Crystal structure of human Glycyl-tRNA synthetase (GlyRS) in complex with AMPCPP · the same entry in another collection · chain A against A, TM-score 1.00
  • P41250 · AlphaFold monomer V2.0 prediction for glycine--tRNA ligase (P41250) · a predicted model of the same protein · chain A against A, TM-score 0.91

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