6l2u
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='6l2u' size='340' side='right'caption='[[6l2u]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='6l2u' size='340' side='right'caption='[[6l2u]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L2U FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=6l2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l2u OCA], [https://pdbe.org/6l2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l2u RCSB], [https://www.ebi.ac.uk/pdbsum/6l2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l2u 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=6l2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l2u OCA], [https://pdbe.org/6l2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l2u RCSB], [https://www.ebi.ac.uk/pdbsum/6l2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l2u ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | By facilitating electron transfer to the hydroxylase diiron center, MMOR-a reductase-serves as an essential component of the catalytic cycle of soluble methane monooxygenase. Here, the X-ray structure analysis of the FAD-binding domain of MMOR identified crucial residues and its influence on the catalytic cycle. | ||
| - | |||
| - | Elucidation of the electron transfer environment in the MMOR FAD-binding domain from Methylosinus sporium 5.,Lee C, Ha SC, Rao Z, Hwang Y, Kim DS, Kim SY, Yoo H, Yoon C, Na JG, Park JH, Lee SJ Dalton Trans. 2021 Nov 23;50(45):16493-16498. doi: 10.1039/d1dt03273a. PMID:34734616<ref>PMID:34734616</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 6l2u" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Acm 3306]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Ha | + | [[Category: Ha SC]] |
| - | [[Category: Kim | + | [[Category: Kim DS]] |
| - | [[Category: Kim | + | [[Category: Kim SY]] |
| - | [[Category: Lee | + | [[Category: Lee SJ]] |
| - | [[Category: Park | + | [[Category: Park JH]] |
| - | [[Category: Rao | + | [[Category: Rao Z]] |
| - | [[Category: Yoo | + | [[Category: Yoo H]] |
| - | [[Category: Yoon | + | [[Category: Yoon C]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Soluble methane monooxygenase reductase FAD-binding domain from Methylosinus sporium.
| |||||||||||
Categories: Large Structures | Ha SC | Kim DS | Kim SY | Lee SJ | Park JH | Rao Z | Yoo H | Yoon C
