9cy2
From Proteopedia
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(New page: '''Unreleased structure''' The entry 9cy2 is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human farnesyl pyrophosphate synthase in complex with a cryptic pocket ligand, JDS05120== | |
| - | + | <StructureSection load='9cy2' size='340' side='right'caption='[[9cy2]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[9cy2]] 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=9CY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CY2 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=JD5:[({5-[4-(CYCLOPROPYLOXY)PHENYL]PYRIDIN-3-YL}AMINO)METHANEDIYL]BIS(PHOSPHONIC+ACID)'>JD5</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=9cy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9cy2 OCA], [https://pdbe.org/9cy2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9cy2 RCSB], [https://www.ebi.ac.uk/pdbsum/9cy2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9cy2 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. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pandya VR]] | ||
| + | [[Category: Park J]] | ||
Current revision
Crystal structure of human farnesyl pyrophosphate synthase in complex with a cryptic pocket ligand, JDS05120
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