› 6fcl

X-ray diffraction
1.5Å resolution

Function and Biology Details

Reaction catalysed: 
AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139738 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenine phosphoribosyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 178 amino acids
Theoretical weight: 19.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07741 (Residues: 3-180; Coverage: 99%)
Gene name: APRT
Sequence domains: Phosphoribosyl transferase domain
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand AMP 2 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P1
Unit cell:
a: 47.55Å b: 47.94Å c: 47.94Å
α: 76.87° β: 61.42° γ: 69.33°
R-values:
R R work R free
0.179 0.178 0.202
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Yeast to Study Human Purine Metabolism Diseases.
Daignan-Fornier et al. (2019)
2 more

1 mention without citation

Structural basis for substrate selectivity and nucleophilic substitution mechanisms in human adenine phosphoribosyltransferase catalyzed reaction.
Ozeir et al. (2019)