6kqb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:39, 22 November 2023) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 6kqb is ON HOLD until Paper Publication
+
==A long chain secondary alcohol dehydrogenase of Micrococcus luteus==
 +
<StructureSection load='6kqb' size='340' side='right'caption='[[6kqb]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[6kqb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Micrococcus_luteus Micrococcus luteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KQB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KQB 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]] 2.261&#8491;</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=6kqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kqb OCA], [https://pdbe.org/6kqb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kqb RCSB], [https://www.ebi.ac.uk/pdbsum/6kqb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kqb ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/A0A4U1L6L9_MICLU A0A4U1L6L9_MICLU]
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Structure-based engineering of a NAD+-dependent secondary alcohol dehydrogenase from Micrococcus luteus led to a 1800-fold increase in catalytic efficiency for NADP+. Furthermore, the engineered enzymes (e.g., D37S/A38R/V39S/T15I) were successfully coupled to a NADPH-dependent Baeyer-Villiger monooxygenase from Pseudomonas putida KT2440 for redox-neutral biotransformations of C18 fatty acids into C9 chemicals.
-
Authors: Kim, H.J., Kim, J.S.
+
Cofactor specificity engineering of a long-chain secondary alcohol dehydrogenase from Micrococcus luteus for redox-neutral biotransformation of fatty acids.,Seo EJ, Kim HJ, Kim MJ, Kim JS, Park JB Chem Commun (Camb). 2019 Nov 28;55(96):14462-14465. doi: 10.1039/c9cc06447h. PMID:31728457<ref>PMID:31728457</ref>
-
Description: A long chain secondary alcohol dehydrogenase of Micrococcus luteus
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
-
[[Category: Kim, J.S]]
+
<div class="pdbe-citations 6kqb" style="background-color:#fffaf0;"></div>
-
[[Category: Kim, H.J]]
+
 
 +
==See Also==
 +
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Micrococcus luteus]]
 +
[[Category: Kim HJ]]
 +
[[Category: Kim JS]]

Current revision

A long chain secondary alcohol dehydrogenase of Micrococcus luteus

PDB ID 6kqb

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools