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Human GAR transformylase in complex with GAR substrate and AGF320 inhibitor

Analyse Human GAR transformylase in complex with GAR substrate and AGF320 inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
8FJX
Type
protein
Length
200 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.17
Source
Homo sapiens
Molecule
Trifunctional purine biosynthetic protein adenosine-3
EC
6.3.4.13, 6.3.3.1, 2.1.2.2
UniProt
P22102
Ligands
Y7L, GAR
Pockets
1 · best druggability 0.64

Structure

x-ray diffraction · resolution 2.17 · 1 distinct chain · 37% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATrifunctional purine biosynthetic protein adenosine-3 (EC 6.3.4.13, 6.3.3.1, 2.1.2.2)protein20037% helix, 24% strandP22102

Ligands and binding sites

  • Y7L · N-{5-[5-(2-amino-4-oxo-3,4-dihydro-5H-pyrrolo[3,2-d]pyrimidin-5-yl)pentyl]thiophene-2-carbonyl}-L-glutamic acid · ligand · chains A
  • GAR · Glycinamide ribonucleotide · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13160.640.8037Y7L, GAR

Compared structures

  • P22102 · AlphaFold monomer V2.0 prediction for trifunctional purine biosynthetic protein… · a predicted model of the same protein · chain A against A, TM-score 0.98

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