PDBe 2gvg

X-ray diffraction
2.2Å resolution

Crystal Structure of human NMPRTase and its complex with NMN

Released:
Source organism: Homo sapiens
Primary publication:
Molecular basis for the inhibition of human NMPRTase, a novel target for anticancer agents.
Nat. Struct. Mol. Biol. 13 582-8 (2006)
PMID: 16783377

Function and Biology Details

Reaction catalysed:
Nicotinamide D-ribonucleotide + diphosphate = nicotinamide + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nicotinamide phosphoribosyltransferase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 491 amino acids
Theoretical weight: 55.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P43490 (Residues: 1-491; Coverage: 100%)
Gene names: NAMPT, PBEF, PBEF1
Sequence domains:
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 253.07Å b: 101.367Å c: 148.2Å
α: 90° β: 125.48° γ: 90°
R-values:
R R work R free
0.197 0.197 0.246
Expression system: Escherichia coli