1GZU: Crystal Structure of Human Nicotinamide Mononucleotide Adenylyltransferase in Complex with NMN

The final step in the biosynthesis of nicotinamide-adenine dinucleotide, a major coenzyme in cellular redox reactions and involved in intracellular signaling, is catalyzed by the enzyme nicotinamide mononucleotide adenylyltransferase (NMNAT). The X-ray structure of human NMNAT in complex with nicotinamide mononucleotide was solved by the single-wavelength anomalous dispersion method at a resolution of 2.9 A. Human NMNAT is a symmetric hexamer whose subunit is formed by a large six-stranded parallel beta-sheet with helices on both sides. Human NMNAT displays a different oligomerization compared to the archaeal enzyme. The protein-nicotinamide mononucleotide interaction pattern provides insight into ligand binding in the human enzyme.
PDB ID: 1GZUDownload
MMDB ID: 20047
PDB Deposition Date: 2002/6/6
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.9  Å
Source Organism:
Similar Structures:
Biological Unit for 1GZU: hexameric; determined by author and by software (PQS)
Molecular Components in 1GZU
Label Count Molecule
Proteins (6 molecules)
Nicotinamide Mononucleotide Adenylyl Transferase(Gene symbol: NMNAT1)
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

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