4kpj

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==Crystal Structure of Farnesyl Pyrophosphate Synthase (Y204A) Mutant complexed with Mg, Pamidronate==
==Crystal Structure of Farnesyl Pyrophosphate Synthase (Y204A) Mutant complexed with Mg, Pamidronate==
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<StructureSection load='4kpj' size='340' side='right' caption='[[4kpj]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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<StructureSection load='4kpj' size='340' side='right'caption='[[4kpj]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4kpj]] 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=4KPJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KPJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4kpj]] 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=4KPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KPJ 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=210:PAMIDRONATE'>210</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.95&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kfa|4kfa]], [[4kpd|4kpd]], [[4kq5|4kq5]], [[4kqs|4kqs]], [[4kqu|4kqu]]</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=210:PAMIDRONATE'>210</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4kpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kpj OCA], [https://pdbe.org/4kpj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kpj RCSB], [https://www.ebi.ac.uk/pdbsum/4kpj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kpj 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=4kpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kpj OCA], [http://pdbe.org/4kpj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kpj RCSB], [http://www.ebi.ac.uk/pdbsum/4kpj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kpj ProSAT]</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.
==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]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Barnett, B L]]
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[[Category: Large Structures]]
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[[Category: Muniz, J R.C]]
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[[Category: Barnett BL]]
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[[Category: Tsoumpra, M K]]
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[[Category: Muniz JRC]]
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[[Category: Walter, R L]]
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[[Category: Tsoumpra MK]]
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[[Category: Bisphosphonate]]
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[[Category: Walter RL]]
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[[Category: Cholesterol synthesis]]
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[[Category: Dimethylallyl pyrophosphate]]
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[[Category: Isoprene biosynthesis]]
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[[Category: Isoprenoid pathway]]
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[[Category: Lipid synthesis]]
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[[Category: Steroid biosynthesis]]
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[[Category: Transferase]]
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Crystal Structure of Farnesyl Pyrophosphate Synthase (Y204A) Mutant complexed with Mg, Pamidronate

PDB ID 4kpj

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