3ua1
From Proteopedia
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| - | [[Image:3ua1.png|left|200px]] | ||
| - | + | ==Crystal structure of the cytochrome P4503A4-bromoergocryptine complex== | |
| - | + | <StructureSection load='3ua1' size='340' side='right'caption='[[3ua1]], [[Resolution|resolution]] 2.15Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3ua1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UA1 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]] 2.15Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=08Y:BROMOERGOCRYPTINE'>08Y</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'>[https://proteopedia.org/fgij/fg.htm?mol=3ua1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ua1 OCA], [https://pdbe.org/3ua1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ua1 RCSB], [https://www.ebi.ac.uk/pdbsum/3ua1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ua1 ProSAT]</span></td></tr> |
| - | [[3ua1]] is a 1 chain structure | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CP3A4_HUMAN CP3A4_HUMAN] Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It performs a variety of oxidation reactions (e.g. caffeine 8-oxidation, omeprazole sulphoxidation, midazolam 1'-hydroxylation and midazolam 4-hydroxylation) of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,8-cineole 2-exo-monooxygenase. The enzyme also hydroxylates etoposide.<ref>PMID:11159812</ref> | ||
==See Also== | ==See Also== | ||
| - | *[[Cytochrome P450|Cytochrome P450]] | + | *[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Poulos TL]] |
| - | [[Category: | + | [[Category: Sevrioukova IF]] |
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Current revision
Crystal structure of the cytochrome P4503A4-bromoergocryptine complex
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