1rby

X-ray diffraction
2.1Å resolution

Human GAR Tfase complex structure with 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid and substrate beta-GAR

Released:
Source organism: Homo sapiens
Entry authors: Zhang Y, Desharnais J, Boger DL, Wilson IA

Function and Biology Details

Reactions catalysed:
10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide
ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-149522 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trifunctional purine biosynthetic protein adenosine-3 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 209 amino acids
Theoretical weight: 22.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22102 (Residues: 808-1010; Coverage: 20%)
Gene names: GART, PGFT, PRGS
Sequence domains: Formyl transferase
Structure domains: Formyl transferase, N-terminal domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P31
Unit cell:
a: 126.171Å b: 126.171Å c: 95.389Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.246 0.245 0.264
Expression system: Escherichia coli