3dbg: Difference between revisions

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<StructureSection load='3dbg' size='340' side='right'caption='[[3dbg]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='3dbg' size='340' side='right'caption='[[3dbg]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3dbg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Strco Strco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DBG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3DBG FirstGlance]. <br>
<table><tr><td colspan='2'>[[3dbg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DBG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 2.6&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3dbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dbg OCA], [http://pdbe.org/3dbg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dbg RCSB], [http://www.ebi.ac.uk/pdbsum/3dbg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3dbg ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=3dbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dbg OCA], [https://pdbe.org/3dbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dbg RCSB], [https://www.ebi.ac.uk/pdbsum/3dbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dbg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/EIZFM_STRCO EIZFM_STRCO]] Involved in the biosynthesis of the sesquiterpenoid antibiotic albaflavenone. Catalyzes the two-step allylic oxidation of epi-isozizaene to albaflavenone. First carries out a non-stereo-specific oxidation of epi-isozizaene to give a mixture of the albaflavenol epimers ((5R)-albaflavenol and (5S)-albaflavenol), each of which can serve as substrate for the second oxidation to yield albaflavenone. This is quite different from most other P450s which catalyze regio- and stereospecific oxidation. Displays also a farnesene synthase activity with farnesyl diphosphate (FPP) as substrate.<ref>PMID:18234666</ref> <ref>PMID:19858213</ref>
[https://www.uniprot.org/uniprot/EIZFM_STRCO EIZFM_STRCO] Involved in the biosynthesis of the sesquiterpenoid antibiotic albaflavenone. Catalyzes the two-step allylic oxidation of epi-isozizaene to albaflavenone. First carries out a non-stereo-specific oxidation of epi-isozizaene to give a mixture of the albaflavenol epimers ((5R)-albaflavenol and (5S)-albaflavenol), each of which can serve as substrate for the second oxidation to yield albaflavenone. This is quite different from most other P450s which catalyze regio- and stereospecific oxidation. Displays also a farnesene synthase activity with farnesyl diphosphate (FPP) as substrate.<ref>PMID:18234666</ref> <ref>PMID:19858213</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/db/3dbg_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/db/3dbg_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Strco]]
[[Category: Vassylyev DG]]
[[Category: Vassylyev, D G]]
[[Category: Waterman MR]]
[[Category: Waterman, M R]]
[[Category: Zhao B]]
[[Category: Zhao, B]]
[[Category: Cyp170a1]]
[[Category: Cytochrome p450 oxidoreductase]]
[[Category: Heme]]
[[Category: Iron]]
[[Category: Metal-binding]]
[[Category: Molecular mechanism]]
[[Category: Monooxygenase]]
[[Category: Oxidoreductase]]
[[Category: Streptomyce]]
Retrieved from "https://proteopedia.org/3dbg"