1io8: Difference between revisions

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<StructureSection load='1io8' size='340' side='right'caption='[[1io8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1io8' size='340' side='right'caption='[[1io8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1io8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IO8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1io8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IO8 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&#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;'>[[1io7|1io7]], [[1io9|1io9]]</div></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=1io8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1io8 OCA], [https://pdbe.org/1io8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1io8 RCSB], [https://www.ebi.ac.uk/pdbsum/1io8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1io8 ProSAT], [https://www.topsan.org/Proteins/RSGI/1io8 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=1io8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1io8 OCA], [https://pdbe.org/1io8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1io8 RCSB], [https://www.ebi.ac.uk/pdbsum/1io8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1io8 ProSAT], [https://www.topsan.org/Proteins/RSGI/1io8 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CP119_SULAC CP119_SULAC]] The endogenous substrate is not known. In vitro, catalyzes the H(2)O(2)-dependent epoxidation of styrene, cis-beta-methylstyrene, and cis-stilbene with retention of stereochemistry. Is able to use cumene hydroperoxide (CHP) or tert-butyl hydroperoxide (TBHP) instead of H(2)O(2) as the electron acceptor. Can also hydroxylate fatty acids such as lauric acid.<ref>PMID:10799487</ref> <ref>PMID:12010041</ref> <ref>PMID:18157853</ref>
[https://www.uniprot.org/uniprot/CP119_SULAC CP119_SULAC] The endogenous substrate is not known. In vitro, catalyzes the H(2)O(2)-dependent epoxidation of styrene, cis-beta-methylstyrene, and cis-stilbene with retention of stereochemistry. Is able to use cumene hydroperoxide (CHP) or tert-butyl hydroperoxide (TBHP) instead of H(2)O(2) as the electron acceptor. Can also hydroxylate fatty acids such as lauric acid.<ref>PMID:10799487</ref> <ref>PMID:12010041</ref> <ref>PMID:18157853</ref>  
== 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: Atcc 35091]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Adachi, S]]
[[Category: Saccharolobus solfataricus]]
[[Category: Park, S Y]]
[[Category: Adachi S]]
[[Category: Structural genomic]]
[[Category: Park S-Y]]
[[Category: Shiro, Y]]
[[Category: Shiro Y]]
[[Category: Sligar, S G]]
[[Category: Sligar SG]]
[[Category: Yamane, K]]
[[Category: Yamane K]]
[[Category: Cytochromo p450]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Oxidoreductase]]
[[Category: Rsgi]]
[[Category: Thermophilic]]

Revision as of 23:34, 27 December 2023

Thermophilic cytochrome P450 (CYP119) from sulfolobus solfataricus: High resolution structural origin of its thermostability and functional properties

1io8, resolution 2.00Å

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