1gzu
From Proteopedia
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CRYSTAL STRUCTURE OF HUMAN NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE IN COMPLEX WITH NMN
Overview
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.
About this Structure
1GZU is a Single protein structure of sequence from Homo sapiens with NMN as ligand. This structure superseeds the now removed PDB entry 1GRY. Active as Nicotinamide-nucleotide adenylyltransferase, with EC number 2.7.7.1 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN., Werner E, Ziegler M, Lerner F, Schweiger M, Heinemann U, FEBS Lett. 2002 Apr 10;516(1-3):239-44. PMID:11959140
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