4jvj

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==Crystal structure of human FPPS in complex with magnesium, CL01131, and sulfate==
==Crystal structure of human FPPS in complex with magnesium, CL01131, and sulfate==
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<StructureSection load='4jvj' size='340' side='right' caption='[[4jvj]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='4jvj' size='340' side='right'caption='[[4jvj]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4jvj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JVJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JVJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4jvj]] 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=4JVJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JVJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1MV:({[6-(4-METHYLPHENYL)THIENO[2,3-D]PYRIMIDIN-4-YL]AMINO}METHANEDIYL)BIS(PHOSPHONIC+ACID)'>1MV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l2x|4l2x]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1MV:({[6-(4-METHYLPHENYL)THIENO[2,3-D]PYRIMIDIN-4-YL]AMINO}METHANEDIYL)BIS(PHOSPHONIC+ACID)'>1MV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jvj OCA], [https://pdbe.org/4jvj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jvj RCSB], [https://www.ebi.ac.uk/pdbsum/4jvj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jvj ProSAT]</span></td></tr>
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<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=4jvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jvj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jvj RCSB], [http://www.ebi.ac.uk/pdbsum/4jvj PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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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[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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4jvj" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Farnesyl diphosphate synthase|Farnesyl diphosphate synthase]]
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*[[Farnesyl diphosphate synthase 3D structures|Farnesyl diphosphate synthase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Berghuis, A M]]
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[[Category: Large Structures]]
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[[Category: Leung, C Y]]
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[[Category: Berghuis AM]]
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[[Category: Park, J]]
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[[Category: Leung C-Y]]
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[[Category: Tsantrizos, Y S]]
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[[Category: Park J]]
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[[Category: Transferase-transferase inhibitor complex]]
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[[Category: Tsantrizos YS]]

Current revision

Crystal structure of human FPPS in complex with magnesium, CL01131, and sulfate

PDB ID 4jvj

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