2ble

X-ray diffraction
1.9Å resolution

Structure of human guanosine monophosphate reductase GMPR1 in complex with GMP

Released:
Source organism: Homo sapiens
Entry authors: Bunkoczi G, Haroniti A, Ng S, von Delft F, Oppermann U, Arrowsmith C, Sundstrom M, Edwards A, Gileadi O

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-153269 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GMP reductase 1 Chain: A
Molecule details ›
Chain: A
Length: 367 amino acids
Theoretical weight: 39.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P36959 (Residues: 1-345; Coverage: 100%)
Gene names: GMPR, GMPR1
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
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P4212
Unit cell:
a: 117.78Å b: 117.78Å c: 54.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.177 0.228
Expression system: Escherichia coli BL21(DE3)