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Crystal structure of human glycyl-tRNA synthetase (glyrs) in complex with AP4A (cocrystallized with AP4A)

Analyse Crystal structure of human glycyl-tRNA synthetase (glyrs) in complex with AP4A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ZXF
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
B4P
Pockets
5 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlycyl-tRNA synthetase (EC 6.1.1.14)protein53034% helix, 21% strandP41250

Ligands and binding sites

  • B4P · Bis(adenosine)-5'-tetraphosphate · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111870.800.8294B4P
2730.440.8123empty
3510.420.8317empty
4530.300.7614empty
5650.280.7315empty

Compared structures

  • 2ZXF · Crystal structure of human glycyl-trna synthetase (GLYRS) in complex with AP4A… · 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 0.92

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