4xqt: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of human FPPS in complex with three magnesium ions==
 
<StructureSection load='4xqt' size='340' side='right' caption='[[4xqt]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
The entry 4xqt is ON HOLD  until Paper Publication
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4xqt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XQT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XQT FirstGlance]. <br>
Authors: Park, J., Berghuis, A.M.
</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=SO4:SULFATE+ION'>SO4</scene></td></tr>
 
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xqr|4xqr]], [[4xqs|4xqs]]</td></tr>
Description: Crystal structure of human FPPS in complex with three magnesium ions
<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=4xqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xqt OCA], [http://pdbe.org/4xqt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xqt RCSB], [http://www.ebi.ac.uk/pdbsum/4xqt PDBsum]</span></td></tr>
[[Category: Unreleased Structures]]
</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.
__TOC__
</StructureSection>
[[Category: Berghuis, A M]]
[[Category: Park, J]]
[[Category: Park, J]]
[[Category: Berghuis, A.M]]
[[Category: Transferase]]

Revision as of 20:14, 20 January 2016

Crystal structure of human FPPS in complex with three magnesium ionsCrystal structure of human FPPS in complex with three magnesium ions

Structural highlights

4xqt is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

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.

4xqt, resolution 2.10Å

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OCA