1zlx

X-ray diffraction
2.2Å resolution

The apo structure of human glycinamide ribonucleotide transformylase

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 Chain: A
Molecule details ›
Chain: A
Length: 203 amino acids
Theoretical weight: 21.94 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

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200, CHESS BEAMLINE F2
Spacegroup: P3221
Unit cell:
a: 75.66Å b: 75.66Å c: 101.69Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.224 0.224 0.267
Expression system: Escherichia coli