› 4o12

X-ray diffraction
2.5Å resolution

Structural and Biochemical Analyses of the Catalysis and Potency Impact of Inhibitor Phosphoribosylation by Human Nicotinamide Phosphoribosyltransferase

Released:
DOI: 10.2210/pdb4o12/pdb
PDB entry 4o12 coloured by chain, front view.
PDB entry 4o12 coloured by chain, side view.
PDB entry 4o12 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and biochemical analyses of the catalysis and potency impact of inhibitor phosphoribosylation by human nicotinamide phosphoribosyltransferase.
Oh A, Ho YC, Zak M, Liu Y, Chen X, Yuen PW, Zheng X, Liu Y, Dragovich PS, Wang W
Chembiochem 15 1121-30 (2014)
PMID: 24797455

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-155082 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nicotinamide phosphoribosyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 501 amino acids
Theoretical weight: 56.94 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:
Ligand 2QG 2 x 2QG
Ligand PO4 3 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P21
Unit cell:
a: 60.57Å b: 106.505Å c: 83.174Å
α: 90° β: 96.64° γ: 90°
R-values:
R R work R free
0.255 0.209 0.255
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance.
Hove-Jensen et al. (2017)
3 more

3 mentions without citation

Superconducting double perovskite bismuth oxide prepared by a low-temperature hydrothermal reaction.
Rubel et al. (2014)
2 more