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1vcf

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<StructureSection load='1vcf' size='340' side='right'caption='[[1vcf]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='1vcf' size='340' side='right'caption='[[1vcf]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1vcf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VCF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1vcf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VCF FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1p0k|1p0k]], [[1p0n|1p0n]], [[1vcg|1vcg]]</div></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Isopentenyl-diphosphate_Delta-isomerase Isopentenyl-diphosphate Delta-isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.2 5.3.3.2] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vcf OCA], [https://pdbe.org/1vcf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vcf RCSB], [https://www.ebi.ac.uk/pdbsum/1vcf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vcf ProSAT], [https://www.topsan.org/Proteins/RSGI/1vcf TOPSAN]</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=1vcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vcf OCA], [https://pdbe.org/1vcf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vcf RCSB], [https://www.ebi.ac.uk/pdbsum/1vcf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vcf ProSAT], [https://www.topsan.org/Proteins/RSGI/1vcf TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/Q746I8_THET2 Q746I8_THET2]] Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP) (By similarity).[HAMAP-Rule:MF_00354]
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[https://www.uniprot.org/uniprot/IDI2_THET2 IDI2_THET2] Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).[HAMAP-Rule:MF_00354]<ref>PMID:17428035</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Isopentenyl-diphosphate delta-isomerase|Isopentenyl-diphosphate delta-isomerase]]
*[[Isopentenyl-diphosphate delta-isomerase|Isopentenyl-diphosphate delta-isomerase]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
 
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[[Category: Isopentenyl-diphosphate Delta-isomerase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Kuramitsu, S]]
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[[Category: Thermus thermophilus]]
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[[Category: Park, S Y]]
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[[Category: Kuramitsu S]]
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[[Category: Structural genomic]]
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[[Category: Park S-Y]]
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[[Category: Tame, R H]]
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[[Category: Tame RH]]
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[[Category: Wada, T]]
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[[Category: Wada T]]
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[[Category: Yokoyama, S]]
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[[Category: Yokoyama S]]
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[[Category: Isomerase]]
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[[Category: Rsgi]]
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[[Category: Tim barrel]]
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Revision as of 00:01, 28 December 2023

Crystal Structure of IPP isomerase at I422

PDB ID 1vcf

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