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X-ray diffraction
2.23Å resolution

complex structure of human GAR Tfase and substrate beta-GAR

Released:

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
Molecule details ›
Chains: A, B, C
Length: 223 amino acids
Theoretical weight: 24.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22102 (Residues: 810-1010; Coverage: 20%)
Gene names: GART, PGFT, PRGS
Sequence domains: Formyl transferase
Structure domains: Formyl transferase, N-terminal domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: R32
Unit cell:
a: 147.825Å b: 147.825Å c: 188.036Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.22 0.266
Expression system: Escherichia coli