5ksx

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Current revision (10:53, 27 September 2023) (edit) (undo)
 
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==Crystal structure of human FPPS in complex with an allosteric inhibitor AM-02-072==
==Crystal structure of human FPPS in complex with an allosteric inhibitor AM-02-072==
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<StructureSection load='5ksx' size='340' side='right' caption='[[5ksx]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
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<StructureSection load='5ksx' size='340' side='right'caption='[[5ksx]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ksx]] 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=5KSX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KSX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ksx]] 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=5KSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KSX 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=7AM:[[(2~{S})-2-[[6-(4-METHYLPHENYL)THIENO[2,3-D]PYRIMIDIN-4-YL]AMINO]-3-PHENYL-PROPANOYL]AMINO]PHOSPHONIC+ACID'>7AM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.65&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7AM:[[(2~{S})-2-[[6-(4-METHYLPHENYL)THIENO[2,3-D]PYRIMIDIN-4-YL]AMINO]-3-PHENYL-PROPANOYL]AMINO]PHOSPHONIC+ACID'>7AM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5ksx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ksx OCA], [http://pdbe.org/5ksx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ksx RCSB], [http://www.ebi.ac.uk/pdbsum/5ksx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ksx ProSAT]</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=5ksx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ksx OCA], [https://pdbe.org/5ksx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ksx RCSB], [https://www.ebi.ac.uk/pdbsum/5ksx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ksx 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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5ksx" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5ksx" style="background-color:#fffaf0;"></div>
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==See Also==
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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: Matralis, A]]
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[[Category: Berghuis AM]]
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[[Category: Park, J]]
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[[Category: Matralis A]]
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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 an allosteric inhibitor AM-02-072

PDB ID 5ksx

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