2vf6: Difference between revisions

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<StructureSection load='2vf6' size='340' side='right'caption='[[2vf6]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='2vf6' size='340' side='right'caption='[[2vf6]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2vf6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VF6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2vf6]] 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=2VF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VF6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M0N:(1-HYDROXY-2-IMIDAZO[1,2-A]PYRIDIN-3-YLETHANE-1,1-DIYL)BIS(PHOSPHONIC+ACID)'>M0N</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.1&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2f92|2f92]], [[2f8c|2f8c]], [[2f9k|2f9k]], [[2f7m|2f7m]], [[1yv5|1yv5]], [[2f89|2f89]], [[2f94|2f94]], [[1zw5|1zw5]], [[1yq7|1yq7]], [[2f8z|2f8z]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M0N:(1-HYDROXY-2-IMIDAZO[1,2-A]PYRIDIN-3-YLETHANE-1,1-DIYL)BIS(PHOSPHONIC+ACID)'>M0N</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dimethylallyltranstransferase Dimethylallyltranstransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.1 2.5.1.1] </span></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=2vf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vf6 OCA], [https://pdbe.org/2vf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vf6 RCSB], [https://www.ebi.ac.uk/pdbsum/2vf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vf6 ProSAT]</span></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=2vf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vf6 OCA], [https://pdbe.org/2vf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vf6 RCSB], [https://www.ebi.ac.uk/pdbsum/2vf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vf6 ProSAT]</span></td></tr>
</table>
</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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dimethylallyltranstransferase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[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: Sgc]]
[[Category: Structural genomic]]
[[Category: Trans-prenyltransferase]]
[[Category: Transferase]]

Latest revision as of 18:18, 13 December 2023

Human FDPS synthase in complex with minodronateHuman FDPS synthase in complex with minodronate

Structural highlights

2vf6 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 2.1Å
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

2vf6, resolution 2.10Å

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