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9yvv
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Cocrystallized structure of Bmp7 in complex with 2,4-dibromophenol== | |
| - | + | <StructureSection load='9yvv' size='340' side='right'caption='[[9yvv]], [[Resolution|resolution]] 2.32Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[9yvv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinomonas_mediterranea Marinomonas mediterranea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9YVV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9YVV 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]] 2.32Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=Y8I:2,4-bis(bromanyl)phenol'>Y8I</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=9yvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9yvv OCA], [https://pdbe.org/9yvv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9yvv RCSB], [https://www.ebi.ac.uk/pdbsum/9yvv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9yvv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/BMP7_MARM1 BMP7_MARM1] Cytochrome P450 protein involved in the biosynthesis of polybrominated aromatic organic compounds (PubMed:25061970). In the presence of ferredoxin, ferredoxin reductase and NADH, catalyzes the coupling of bromophenols and bromopyrroles, forming various polybrominated biphenyls and hydroxylated polybrominated diphenyl ethers (OH-BDE) (By similarity). Can also mediate the heterocoupling of 3,5-dibromocatechol, forming six different compounds, including polybrominated dibenzo-p-dioxins, which are among the most toxic molecules known to man (PubMed:25061970).[UniProtKB:V4HJ73]<ref>PMID:25061970</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Marinomonas mediterranea]] | ||
| + | [[Category: Nolan K]] | ||
| + | [[Category: Wang Y]] | ||
Current revision
Cocrystallized structure of Bmp7 in complex with 2,4-dibromophenol
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