4kfa
From Proteopedia
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==Crystal structure of human farnesyl pyrophosphate synthase (t201a mutant) complexed with mg and zoledronate== | ==Crystal structure of human farnesyl pyrophosphate synthase (t201a mutant) complexed with mg and zoledronate== | ||
<StructureSection load='4kfa' size='340' side='right' caption='[[4kfa]], [[Resolution|resolution]] 1.98Å' scene=''> | <StructureSection load='4kfa' size='340' side='right' caption='[[4kfa]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zw5|1zw5]], [[2vf6|2vf6]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zw5|1zw5]], [[2vf6|2vf6]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FDPS, FPS, KIAA1293 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FDPS, FPS, KIAA1293 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4kfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kfa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kfa RCSB], [http://www.ebi.ac.uk/pdbsum/4kfa 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=4kfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kfa OCA], [http://pdbe.org/4kfa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kfa RCSB], [http://www.ebi.ac.uk/pdbsum/4kfa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kfa ProSAT]</span></td></tr> |
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== Function == | == Function == | ||
[[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. | [[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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| + | ==See Also== | ||
| + | *[[Farnesyl diphosphate synthase|Farnesyl diphosphate synthase]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 21:45, 4 August 2016
Crystal structure of human farnesyl pyrophosphate synthase (t201a mutant) complexed with mg and zoledronate
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Categories: Human | Barnett, B L | Muniz, J R.C | Tsoumpra, M K | Walter, R L | Bisphosphonate | Cholesterol synthesis | Isopentyl pyrophosphate and dimethylallyl pyrophosphate | Isoprene biosynthesis | Isoprenoid pathway | Lipid synthesis | Steroid biosynthesis | Transferase | Transferase-transferase inhibitor complex
