3r1a
From Proteopedia
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| - | [[Image:3r1a.png|left|200px]] | ||
| - | + | ==Closed crystal structure of cytochrome P450 2B4 covalently bound to the mechanism-based inactivator tert-butylphenylacetylene== | |
| - | + | <StructureSection load='3r1a' size='340' side='right'caption='[[3r1a]], [[Resolution|resolution]] 3.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3r1a]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R1A FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</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>, <scene name='pdbligand=TB2:(4-TERT-BUTYLPHENYL)ACETALDEHYDE'>TB2</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=3r1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r1a OCA], [https://pdbe.org/3r1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r1a RCSB], [https://www.ebi.ac.uk/pdbsum/3r1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r1a ProSAT]</span></td></tr> |
| - | [[3r1a]] is a 8 chain structure | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CP2B4_RABIT CP2B4_RABIT] Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. In the epoxidation of arachidonic acid it has a unique preference for the 5,6-olefin. | ||
==See Also== | ==See Also== | ||
| - | *[[Cytochrome P450|Cytochrome P450]] | + | *[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]] |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
| - | + | [[Category: Gay SC]] | |
| - | [[Category: Gay | + | [[Category: Halpert JR]] |
| - | [[Category: Halpert | + | [[Category: Hollenberg PF]] |
| - | [[Category: Hollenberg | + | [[Category: Stout CD]] |
| - | [[Category: Stout | + | [[Category: Zhang H]] |
| - | [[Category: Zhang | + | |
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Current revision
Closed crystal structure of cytochrome P450 2B4 covalently bound to the mechanism-based inactivator tert-butylphenylacetylene
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