4n9u

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==The role of lysine 200 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates==
==The role of lysine 200 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates==
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<StructureSection load='4n9u' size='340' side='right' caption='[[4n9u]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
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<StructureSection load='4n9u' size='340' side='right'caption='[[4n9u]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4n9u]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N9U FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4n9u]] 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=4N9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N9U 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=RIS:1-HYDROXY-2-(3-PYRIDINYL)ETHYLIDENE+BIS-PHOSPHONIC+ACID'>RIS</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]] 2.11&#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]], [[4kpj|4kpj]], [[4kq5|4kq5]], [[4kqs|4kqs]], [[4kqu|4kqu]], [[1yq7|1yq7]], [[4nua|4nua]], [[4ng6|4ng6]], [[4nke|4nke]], [[4nkf|4nkf]]</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=RIS:1-HYDROXY-2-(3-PYRIDINYL)ETHYLIDENE+BIS-PHOSPHONIC+ACID'>RIS</scene></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=4n9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n9u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n9u RCSB], [http://www.ebi.ac.uk/pdbsum/4n9u PDBsum]</span></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=4n9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n9u OCA], [https://pdbe.org/4n9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n9u RCSB], [https://www.ebi.ac.uk/pdbsum/4n9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n9u ProSAT]</span></td></tr>
</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.
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==See Also==
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*[[Farnesyl diphosphate synthase 3D structures|Farnesyl diphosphate synthase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Barnett, B L]]
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[[Category: Homo sapiens]]
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[[Category: Dunford, J E]]
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[[Category: Large Structures]]
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[[Category: Ebetino, F H]]
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[[Category: Barnett BL]]
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[[Category: Evdokimov, A]]
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[[Category: Dunford JE]]
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[[Category: Kavanagh, K L]]
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[[Category: Ebetino FH]]
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[[Category: Kwaasi, A A]]
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[[Category: Evdokimov A]]
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[[Category: Muniz, J R.C]]
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[[Category: Kavanagh KL]]
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[[Category: Oppermann, U]]
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[[Category: Kwaasi AA]]
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[[Category: Pilka, E]]
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[[Category: Muniz JRC]]
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[[Category: Russell, R G.G]]
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[[Category: Oppermann U]]
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[[Category: Tsoumpra, M K]]
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[[Category: Pilka E]]
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[[Category: Walter, R L]]
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[[Category: Russell RGG]]
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[[Category: Alpha-helical prenyltransferase fold]]
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[[Category: Tsoumpra MK]]
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[[Category: Dimethylallyl pyrophosphate]]
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[[Category: Walter RL]]
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[[Category: Isopentenyl pyrophosphate]]
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[[Category: Isoprene biosynthesis]]
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[[Category: Lipid synthesis]]
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[[Category: Steroid biosynthesis]]
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[[Category: Transferase]]
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Current revision

The role of lysine 200 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates

PDB ID 4n9u

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