4nke

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<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=4nke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nke OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nke RCSB], [http://www.ebi.ac.uk/pdbsum/4nke PDBsum]</span></td></tr>
<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=4nke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nke OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nke RCSB], [http://www.ebi.ac.uk/pdbsum/4nke PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/FPPS_HUMAN FPPS_HUMAN]] Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.
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</StructureSection>
</StructureSection>

Revision as of 17:31, 24 December 2014

The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates

4nke, resolution 1.46Å

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