› 2bzn

X-ray diffraction
2.15Å resolution

Crystal structure of human guanosine monophosphate reductase 2 GMPR2 in complex with IMP

Released:
DOI: 10.2210/pdb2bzn/pdb
PDB entry 2bzn coloured by chain, front view.
PDB entry 2bzn coloured by chain, side view.
PDB entry 2bzn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cofactor mobility determines reaction outcome in the IMPDH and GMPR (β-α)8 barrel enzymes.
Patton GC, Stenmark P, Gollapalli DR, Sevastik R, Kursula P, Flodin S, Schuler H, Swales CT, Eklund H, Himo F, Nordlund P, Hedstrom L
Nat Chem Biol 7 950-8 (2011)
PMID: 22037469

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192846 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GMP reductase 2 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 351 amino acids
Theoretical weight: 38.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9P2T1 (Residues: 9-341; Coverage: 96%)
Gene name: GMPR2
Sequence domains: IMP dehydrogenase / GMP reductase domain
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand IMP 8 x IMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 131.291Å b: 141.35Å c: 164.895Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.158 0.21
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Functional diversity of organic molecule enzyme cofactors.
Richter M. (2013)
1 more

3 mentions without citation

The dynamic determinants of reaction specificity in the IMPDH/GMPR family of (β/α)(8) barrel enzymes.
Hedstrom L. (2012)
2 more