1gzu
From Proteopedia
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|PDB= 1gzu |SIZE=350|CAPTION= <scene name='initialview01'>1gzu</scene>, resolution 2.90Å | |PDB= 1gzu |SIZE=350|CAPTION= <scene name='initialview01'>1gzu</scene>, resolution 2.90Å | ||
|SITE= <scene name='pdbsite=NMA:Nmn+Binding+Site+For+Chain+C'>NMA</scene> | |SITE= <scene name='pdbsite=NMA:Nmn+Binding+Site+For+Chain+C'>NMA</scene> | ||
| - | |LIGAND= <scene name='pdbligand=NMN:BETA-NICOTINAMIDE RIBOSE MONOPHOSPHATE'>NMN</scene> | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NMN:BETA-NICOTINAMIDE+RIBOSE+MONOPHOSPHATE'>NMN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Nicotinamide-nucleotide_adenylyltransferase Nicotinamide-nucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.1 2.7.7.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinamide-nucleotide_adenylyltransferase Nicotinamide-nucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.1 2.7.7.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gzu OCA], [http://www.ebi.ac.uk/pdbsum/1gzu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gzu RCSB]</span> | ||
}} | }} | ||
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[[Category: Werner, E.]] | [[Category: Werner, E.]] | ||
[[Category: Ziegler, M.]] | [[Category: Ziegler, M.]] | ||
| - | [[Category: NMN]] | ||
[[Category: adenylyltransferase]] | [[Category: adenylyltransferase]] | ||
[[Category: nad biosynthesis]] | [[Category: nad biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:54:56 2008'' |
Revision as of 17:55, 30 March 2008
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| , resolution 2.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Nicotinamide-nucleotide adenylyltransferase, with EC number 2.7.7.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. This structure supersedes the now removed PDB entry 1GRY. 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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