2rah: Difference between revisions

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[[Image:2rah.jpg|left|200px]]


{{Structure
==Human FDPS synthase in complex with novel inhibitor==
|PDB= 2rah |SIZE=350|CAPTION= <scene name='initialview01'>2rah</scene>, resolution 2.000&Aring;
<StructureSection load='2rah' size='340' side='right'caption='[[2rah]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=11P:[(7R)-6,7-DIHYDRO-5H-CYCLOPENTA[C]PYRIDIN-7-YL(HYDROXY)METHYLENE]BIS(PHOSPHONIC+ACID)'>11P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<table><tr><td colspan='2'>[[2rah]] 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=2RAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RAH FirstGlance]. <br>
|ACTIVITY=  
</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&#8491;</td></tr>
|GENE= FDPS, FPS, KIAA1293 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=11P:[(7R)-6,7-DIHYDRO-5H-CYCLOPENTA[C]PYRIDIN-7-YL(HYDROXY)METHYLENE]BIS(PHOSPHONIC+ACID)'>11P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rah OCA], [https://pdbe.org/2rah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rah RCSB], [https://www.ebi.ac.uk/pdbsum/2rah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rah ProSAT]</span></td></tr>
|RELATEDENTRY=[[1zw5|1ZW5]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rah OCA], [http://www.ebi.ac.uk/pdbsum/2rah PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2rah RCSB]</span>
== 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/ra/2rah_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=2rah ConSurf].
<div style="clear:both"></div>


'''Human FDPS synthase in complex with novel inhibitor'''
==See Also==
 
*[[Farnesyl diphosphate synthase 3D structures|Farnesyl diphosphate synthase 3D structures]]
 
__TOC__
==About this Structure==
</StructureSection>
2RAH is a [[Single protein]] 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=2RAH OCA].
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Barnett, B L.]]
[[Category: Barnett BL]]
[[Category: Ebetino, F H.]]
[[Category: Ebetino FH]]
[[Category: Evdokimov, A G.]]
[[Category: Evdokimov AG]]
[[Category: Pokross, M.]]
[[Category: Pokross M]]
[[Category: cholesterol biosynthesis]]
[[Category: cytoplasm]]
[[Category: host-virus interaction]]
[[Category: isoprene biosynthesis]]
[[Category: lipid synthesis]]
[[Category: mainly alpha]]
[[Category: orthogonal bundle]]
[[Category: osteoporosis]]
[[Category: steroid biosynthesis]]
[[Category: sterol biosynthesis]]
[[Category: transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:58:14 2008''

Latest revision as of 14:52, 30 August 2023

Human FDPS synthase in complex with novel inhibitorHuman FDPS synthase in complex with novel inhibitor

Structural highlights

2rah 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 2Å
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

2rah, resolution 2.00Å

Drag the structure with the mouse to rotate

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OCA
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