This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3n5h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "3n5h" [edit=sysop:move=sysop])

Revision as of 20:45, 17 April 2013

Template:STRUCTURE 3n5h

Contents

Human fpps complex with NOV_304

Template:ABSTRACT PUBMED 20711197

Function

[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.

About this Structure

3n5h is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Jahnke W, Rondeau JM, Cotesta S, Marzinzik A, Pelle X, Geiser M, Strauss A, Gotte M, Bitsch F, Hemmig R, Henry C, Lehmann S, Glickman JF, Roddy TP, Stout SJ, Green JR. Allosteric non-bisphosphonate FPPS inhibitors identified by fragment-based discovery. Nat Chem Biol. 2010 Sep;6(9):660-6. Epub 2010 Aug 15. PMID:20711197 doi:10.1038/nchembio.421

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools