2a7r

X-ray diffraction
3Å resolution

Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)

Released:

Function and Biology Details

Reaction catalysed:
Inosine 5'-phosphate + NH(3) + NADP(+) = guanosine 5'-phosphate + NADPH
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-192846 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GMP reductase 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 366 amino acids
Theoretical weight: 39.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9P2T1 (Residues: 1-348; Coverage: 100%)
Gene name: GMPR2
Sequence domains: IMP dehydrogenase / GMP reductase domain
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 110.56Å b: 110.56Å c: 209.75Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.233 0.228 0.276
Expression system: Escherichia coli