PDBe 3dgr

X-ray diffraction
2.1Å resolution

Crystal structure of human NAMPT complexed with ADP analogue

Released:
Source organism: Homo sapiens
Primary publication:
A phosphoenzyme mimic, overlapping catalytic sites and reaction coordinate motion for human NAMPT.
Proc. Natl. Acad. Sci. U.S.A. 106 13748-53 (2009)
PMID: 19666527

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
Molecule details ›
Chains: A, B
Length: 484 amino acids
Theoretical weight: 54.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P43490 (Residues: 1-484; Coverage: 99%)
Gene names: NAMPT, PBEF, PBEF1
Sequence domains:
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 61.29Å b: 107.229Å c: 82.661Å
α: 90° β: 96.41° γ: 90°
R-values:
R R work R free
0.182 0.18 0.225
Expression system: Escherichia coli