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Human gar transformylase in complex with gar and (4-{[2-(2-amino-4- oxo-4,7-dihydro-3H-PYRROLO[2,3-D]PYRIMIDIN-6-YL)ETHYL]AMINO}BENZOYL)- L-glutamic acid (AGF183)

Analyse Human gar transformylase in complex with gar and (4-{[2-(2-amino-4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5J9F
Type
protein
Length
200 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Trifunctional purine biosynthetic protein adenosine-3
EC
6.3.4.13, 6.3.3.1, 2.1.2.2
UniProt
P22102
Ligands
GAR, 83A
Pockets
1 · best druggability 0.65

Structure

x-ray diffraction · 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

  • GAR · Glycinamide ribonucleotide · ligand · chains A
  • 83A · N-(4-{[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)ethyl]amino}benzene-1-carbonyl)-L-glutamic acid · 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
13140.650.8136GAR, 83A

Compared structures

  • 5J9F · Human GAR transformylase in complex with GAR and… · the same entry in another collection · chain A against A, TM-score 1.00
  • P22102 · AlphaFold monomer V2.0 prediction for trifunctional purine biosynthetic protein… · a predicted model of the same protein · chain A against A, TM-score 0.99

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