4kfa

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==Crystal structure of human farnesyl pyrophosphate synthase (t201a mutant) complexed with mg and zoledronate==
==Crystal structure of human farnesyl pyrophosphate synthase (t201a mutant) complexed with mg and zoledronate==
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<StructureSection load='4kfa' size='340' side='right' caption='[[4kfa]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
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<StructureSection load='4kfa' size='340' side='right'caption='[[4kfa]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4kfa]] 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=4KFA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KFA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4kfa]] 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=4KFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KFA 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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZOL:ZOLEDRONIC+ACID'>ZOL</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZOL:ZOLEDRONIC+ACID'>ZOL</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zw5|1zw5]], [[2vf6|2vf6]]</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=4kfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kfa OCA], [https://pdbe.org/4kfa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kfa RCSB], [https://www.ebi.ac.uk/pdbsum/4kfa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kfa ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4kfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kfa OCA], [http://pdbe.org/4kfa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kfa RCSB], [http://www.ebi.ac.uk/pdbsum/4kfa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kfa 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: Isopentyl pyrophosphate and 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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[[Category: Transferase-transferase inhibitor complex]]
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Revision as of 11:55, 30 November 2022

Crystal structure of human farnesyl pyrophosphate synthase (t201a mutant) complexed with mg and zoledronate

PDB ID 4kfa

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