4h5d: Difference between revisions

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 ==Crystal structure of human FPPS in ternary complex with YS0470 and inorganic pyrophosphate==
-<StructureSection load='4h5d' size='340' side='right' caption='[[4h5d]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
+<StructureSection load='4h5d' size='340' side='right'caption='[[4h5d]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4h5d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H5D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4h5d]] 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=4H5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H5D FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=YS4:[({4-[4-(PROPAN-2-YLOXY)PHENYL]PYRIDIN-2-YL}AMINO)METHANEDIYL]BIS(PHOSPHONIC+ACID)'>YS4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.02&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dem|4dem]], [[4h5c|4h5c]], [[4h5e|4h5e]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=YS4:[({4-[4-(PROPAN-2-YLOXY)PHENYL]PYRIDIN-2-YL}AMINO)METHANEDIYL]BIS(PHOSPHONIC+ACID)'>YS4</scene></td></tr>
-<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 Homo sapiens])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4h5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h5d OCA], [https://pdbe.org/4h5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h5d RCSB], [https://www.ebi.ac.uk/pdbsum/4h5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h5d ProSAT]</span></td></tr>
-<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=4h5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h5d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h5d RCSB], [http://www.ebi.ac.uk/pdbsum/4h5d PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[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.
+[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;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4h5d" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Farnesyl diphosphate synthase|Farnesyl diphosphate synthase]]
+*[[Farnesyl diphosphate synthase 3D structures|Farnesyl diphosphate synthase 3D structures]]
 == References ==
 <references/>
@@ Line 26: / Line 27: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Berghuis, A M]]
+[[Category: Large Structures]]
-[[Category: Lin, Y S]]
+[[Category: Berghuis AM]]
-[[Category: Park, J]]
+[[Category: Lin Y-S]]
-[[Category: Tsantrizos, Y S]]
+[[Category: Park J]]
-[[Category: Transferase]]
+[[Category: Tsantrizos YS]]
-[[Category: Transferase-transferase inhibitor complex]]