3cp6: Difference between revisions

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[[Image:3cp6.png|left|200px]]


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==Crystal structure of human farnesyl diphosphate synthase (T201A mutant) complexed with Mg and biphosphonate inhibitor==
The line below this paragraph, containing "STRUCTURE_3cp6", creates the "Structure Box" on the page.
<StructureSection load='3cp6' size='340' side='right'caption='[[3cp6]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3cp6]] 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=3CP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CP6 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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='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=RSX:(4AS,7AR)-OCTAHYDRO-1H-CYCLOPENTA[B]PYRIDINE-6,6-DIYLBIS(PHOSPHONIC+ACID)'>RSX</scene></td></tr>
{{STRUCTURE_3cp6| PDB=3cp6 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cp6 OCA], [https://pdbe.org/3cp6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cp6 RCSB], [https://www.ebi.ac.uk/pdbsum/3cp6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cp6 ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cp/3cp6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cp6 ConSurf].
<div style="clear:both"></div>


===Crystal structure of human farnesyl diphosphate synthase (T201A mutant) complexed with Mg and biphosphonate inhibitor===
==See Also==
 
*[[Farnesyl diphosphate synthase 3D structures|Farnesyl diphosphate synthase 3D structures]]
 
__TOC__
==About this Structure==
</StructureSection>
3CP6 is a 1 chain structure of 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=3CP6 OCA].
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C H.]]
[[Category: Large Structures]]
[[Category: Barnett, B L.]]
[[Category: Arrowsmith CH]]
[[Category: Bountra, C.]]
[[Category: Barnett BL]]
[[Category: Delft, F von.]]
[[Category: Bountra C]]
[[Category: Dunford, J E.]]
[[Category: Dunford JE]]
[[Category: Ebetino, F H.]]
[[Category: Ebetino FH]]
[[Category: Edwards, A M.]]
[[Category: Edwards AM]]
[[Category: Guo, K.]]
[[Category: Guo K]]
[[Category: Oppermann, U.]]
[[Category: Oppermann U]]
[[Category: Pike, A C.W.]]
[[Category: Pike ACW]]
[[Category: Pilka, E S.]]
[[Category: Pilka ES]]
[[Category: Russell, R G.G.]]
[[Category: Russell RGG]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Von Delft F]]
[[Category: Bisphosphonate]]
[[Category: Cholesterol biosynthesis]]
[[Category: Cholesterol synthesis]]
[[Category: Cytoplasm]]
[[Category: Host-virus interaction isoprene biosynthesis]]
[[Category: Isoprenoid pathway]]
[[Category: Lipid synthesis]]
[[Category: Sgc]]
[[Category: Steroid biosynthesis]]
[[Category: Sterol biosynthesis]]
[[Category: Structural genomic]]
[[Category: Structural genomics consortium]]
[[Category: Transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 06:24:43 2009''

Latest revision as of 17:56, 20 September 2023

Crystal structure of human farnesyl diphosphate synthase (T201A mutant) complexed with Mg and biphosphonate inhibitorCrystal structure of human farnesyl diphosphate synthase (T201A mutant) complexed with Mg and biphosphonate inhibitor

Structural highlights

3cp6 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.95Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

3cp6, resolution 1.95Å

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