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==X-ray Crystal Structure of CYP119 complexed with 4-(4-flourophenyl)-1H-imidazole==
==X-ray Crystal Structure of CYP119 complexed with 4-(4-flourophenyl)-1H-imidazole==
<StructureSection load='4wpd' size='340' side='right' caption='[[4wpd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4wpd' size='340' side='right'caption='[[4wpd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4wpd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WPD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WPD FirstGlance]. <br>
<table><tr><td colspan='2'>[[4wpd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius_DSM_639 Sulfolobus acidocaldarius DSM 639]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WPD FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3SQ:4-(4-FLUOROPHENYL)-1H-IMIDAZOLE'>3SQ</scene>, <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]] 2.001&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tt5|4tt5]], [[4tuv|4tuv]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3SQ:4-(4-FLUOROPHENYL)-1H-IMIDAZOLE'>3SQ</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wpd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wpd RCSB], [http://www.ebi.ac.uk/pdbsum/4wpd PDBsum]</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=4wpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wpd OCA], [https://pdbe.org/4wpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wpd RCSB], [https://www.ebi.ac.uk/pdbsum/4wpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wpd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>  
 
==See Also==
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Madrona, Y]]
[[Category: Large Structures]]
[[Category: Cytochrome p450]]
[[Category: Sulfolobus acidocaldarius DSM 639]]
[[Category: Oxidoreductase]]
[[Category: Madrona Y]]

Latest revision as of 03:54, 28 December 2023

X-ray Crystal Structure of CYP119 complexed with 4-(4-flourophenyl)-1H-imidazoleX-ray Crystal Structure of CYP119 complexed with 4-(4-flourophenyl)-1H-imidazole

Structural highlights

4wpd is a 2 chain structure with sequence from Sulfolobus acidocaldarius DSM 639. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.001Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3]

See Also

References

  1. ↑ Koo LS, Tschirret-Guth RA, Straub WE, Moenne-Loccoz P, Loehr TM, Ortiz de Montellano PR. The active site of the thermophilic CYP119 from Sulfolobus solfataricus. J Biol Chem. 2000 May 12;275(19):14112-23. PMID:10799487
  2. ↑ Koo LS, Immoos CE, Cohen MS, Farmer PJ, Ortiz de Montellano PR. Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119. J Am Chem Soc. 2002 May 22;124(20):5684-91. PMID:12010041
  3. ↑ Rabe KS, Kiko K, Niemeyer CM. Characterization of the peroxidase activity of CYP119, a thermostable P450 from Sulfolobus acidocaldarius. Chembiochem. 2008 Feb 15;9(3):420-5. PMID:18157853 doi:http://dx.doi.org/10.1002/cbic.200700450

4wpd, resolution 2.00Å

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