5lx5: Difference between revisions
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==CRYSTAL STRUCTURE OF VISFATIN IN COMPLEX WITH SAR154782-RP.== | |||
<StructureSection load='5lx5' size='340' side='right' caption='[[5lx5]], [[Resolution|resolution]] 1.88Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5lx5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LX5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LX5 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7A0:[(2~{R},3~{S},4~{R},5~{R})-5-[2-azanyl-5-[[[4-[6-(ethylamino)-5-(2-piperidin-1-ylethylcarbamoyl)pyridin-2-yl]-2-fluoranyl-phenyl]carbamoylamino]methyl]pyridin-1-ium-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl+dihydrogen+phosphate'>7A0</scene>, <scene name='pdbligand=DPO:DIPHOSPHATE'>DPO</scene></td></tr> | |||
[[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinamide_phosphoribosyltransferase Nicotinamide phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.12 2.4.2.12] </span></td></tr> | ||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5lx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lx5 OCA], [http://pdbe.org/5lx5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lx5 RCSB], [http://www.ebi.ac.uk/pdbsum/5lx5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lx5 ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/NAMPT_HUMAN NAMPT_HUMAN]] Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway (By similarity). | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Nicotinamide phosphoribosyltransferase]] | |||
[[Category: Bertrand, T]] | [[Category: Bertrand, T]] | ||
[[Category: Marquette, J P]] | |||
[[Category: Cancer]] | |||
[[Category: Drug design]] | |||
[[Category: Inhibitor]] | |||
[[Category: Nampt]] | |||
[[Category: Transferase]] | |||
Revision as of 10:11, 25 October 2017
CRYSTAL STRUCTURE OF VISFATIN IN COMPLEX WITH SAR154782-RP.CRYSTAL STRUCTURE OF VISFATIN IN COMPLEX WITH SAR154782-RP.
Structural highlights
Function[NAMPT_HUMAN] Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway (By similarity). |
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