This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3rwl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:45, 1 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3rwl' size='340' side='right'caption='[[3rwl]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3rwl' size='340' side='right'caption='[[3rwl]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3rwl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_51380 Atcc 51380]. 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>
+
<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='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>
+
</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&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ahpG1, Sphingomonas sp. ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33050 ATCC 51380])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alkane_1-monooxygenase Alkane 1-monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.3 1.14.15.3] </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=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>
<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>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/Q5F4D9_SPHMC Q5F4D9_SPHMC]
-
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&reg;/PubMed&reg;, 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__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Alkane 1-monooxygenase]]
 
-
[[Category: Atcc 51380]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Pompidor, G]]
+
[[Category: Sphingopyxis macrogoltabida]]
-
[[Category: Oxidoreductase]]
+
[[Category: Pompidor G]]
-
[[Category: P450 monooxygenase]]
+

Current revision

Structure of P450pyr hydroxylase

PDB ID 3rwl

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools