3s4j: Difference between revisions
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New page: '''Unreleased structure''' The entry 3s4j is ON HOLD Authors: Evdokimov, A.G., Barnett, B.L., Ebetino, F.H., Pokross, M. Description: Human FDPS Synthase in Complex with a Rigid Analog... |
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==Human FDPS Synthase in Complex with a Rigid Analog of Risedronate== | |||
<StructureSection load='3s4j' size='340' side='right'caption='[[3s4j]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3s4j]] 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=3S4J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S4J 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]] 1.95Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNV:6,7-DIHYDRO-5H-CYCLOPENTA[B]PYRIDINE-6,6-DIYLBIS(PHOSPHONIC+ACID)'>UNV</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=3s4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s4j OCA], [https://pdbe.org/3s4j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s4j RCSB], [https://www.ebi.ac.uk/pdbsum/3s4j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s4j 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__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Barnett BL]] | |||
[[Category: Ebetino FH]] | |||
[[Category: Evdokimov AG]] | |||
[[Category: Pokross M]] | |||
Latest revision as of 15:46, 14 March 2024
Human FDPS Synthase in Complex with a Rigid Analog of RisedronateHuman FDPS Synthase in Complex with a Rigid Analog of Risedronate
Structural highlights
FunctionFPPS_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 |
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