› 2gvl

X-ray diffraction
2.1Å resolution

Crystal Structure of Murine NMPRTase

Released:
DOI: 10.2210/pdb2gvl/pdb
PDB entry 2gvl coloured by chain, front view.
PDB entry 2gvl coloured by chain, side view.
PDB entry 2gvl coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Molecular basis for the inhibition of human NMPRTase, a novel target for anticancer agents.
Khan JA, Tao X, Tong L
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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189340 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nicotinamide phosphoribosyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 491 amino acids
Theoretical weight: 55.57 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99KQ4 (Residues: 1-491; Coverage: 100%)
Gene names: Nampt, Pbef1
Sequence domains:
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 2 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21
Unit cell:
a: 60.263Å b: 107.736Å c: 83.287Å
α: 90° β: 96.57° γ: 90°
R-values:
R R work R free
0.228 0.225 0.27
Expression system: Escherichia coli

Quick links

Citations

33 review citations

Nampt: linking NAD biology, metabolism and cancer.
Garten et al. (2009)
32 more

2 mentions without citation

A phosphoenzyme mimic, overlapping catalytic sites and reaction coordinate motion for human NAMPT.
Burgos et al. (2009)
1 more