5cg5
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Neutron crystal structure of human farnesyl pyrophosphate synthase in complex with risedronate== | |
| + | <StructureSection load='5cg5' size='340' side='right'caption='[[5cg5]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5cg5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CG5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Hybrid , Neutron Diffraction , X-ray diffraction, [[Resolution|Resolution]] 1.402Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=RIS:1-HYDROXY-2-(3-PYRIDINYL)ETHYLIDENE+BIS-PHOSPHONIC+ACID'>RIS</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5cg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cg5 OCA], [https://pdbe.org/5cg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cg5 RCSB], [https://www.ebi.ac.uk/pdbsum/5cg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cg5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://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. | ||
| - | + | ==See Also== | |
| - | + | *[[Farnesyl diphosphate synthase 3D structures|Farnesyl diphosphate synthase 3D structures]] | |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Niimura | + | [[Category: Kusaka K]] |
| - | [[Category: | + | [[Category: Mizuguchi M]] |
| - | [[Category: | + | [[Category: Niimura N]] |
| - | [[Category: | + | [[Category: Ostermann A]] |
| - | [[Category: | + | [[Category: Schrader TE]] |
| + | [[Category: Tanaka I]] | ||
| + | [[Category: Yokoyama T]] | ||
Current revision
Neutron crystal structure of human farnesyl pyrophosphate synthase in complex with risedronate
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