4nkf

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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=4nkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nkf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nkf RCSB], [http://www.ebi.ac.uk/pdbsum/4nkf 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=4nkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nkf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nkf RCSB], [http://www.ebi.ac.uk/pdbsum/4nkf 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 23:41, 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

4nkf, resolution 2.00Å

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