2bwg

X-ray diffraction
2.4Å 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, Gileadi O, Oppermann U, Arrowsmith C, Edwards A, Sundstrom M

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GMP reductase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
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: RIGAKU FR-E
Spacegroup: P21
Unit cell:
a: 55.312Å b: 114.418Å c: 115.129Å
α: 90° β: 102.74° γ: 90°
R-values:
R R work R free
0.199 0.196 0.245
Expression system: Escherichia coli BL21(DE3)