3rwl: Difference between revisions
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New page: '''Unreleased structure''' The entry 3rwl is ON HOLD Authors: Pompidor, G. Description: Structure of P450pyr hydrolase |
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==Structure of P450pyr hydroxylase== | |||
<StructureSection load='3rwl' size='340' side='right'caption='[[3rwl]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3rwl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingopyxis_macrogoltabida Sphingopyxis macrogoltabida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RWL 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]] 2Å</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=3rwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rwl OCA], [https://pdbe.org/3rwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rwl RCSB], [https://www.ebi.ac.uk/pdbsum/3rwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rwl ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5F4D9_SPHMC Q5F4D9_SPHMC] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Directed evolution of a monooxygenase to achieve very high enantioselectivity for hydroxylation at non-activated carbon atoms is demonstrated for the first time, where a triple mutant of P450pyr hydroxylase is obtained via determination of enzyme structure, iterative saturation mutagenesis, and high-throughput screening with a MS-based ee assay to increase the product ee from 53% to 98% for the hydroxylation of N-benzyl pyrrolidine to (S)-N-benzyl 3-hydroxypyrrolidine. | |||
Evolving P450pyr hydroxylase for highly enantioselective hydroxylation at non-activated carbon atom.,Pham SQ, Pompidor G, Liu J, Li XD, Li Z Chem Commun (Camb). 2012 May 14;48(38):4618-20. Epub 2012 Mar 19. PMID:22430002<ref>PMID:22430002</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3rwl" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sphingopyxis macrogoltabida]] | |||
[[Category: Pompidor G]] | |||
