2m6s
From Proteopedia
(Difference between revisions)
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==Holo_YqcA== | ==Holo_YqcA== | ||
- | <StructureSection load='2m6s' size='340' side='right'caption='[[2m6s | + | <StructureSection load='2m6s' size='340' side='right'caption='[[2m6s]]' 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=2M6S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M6S FirstGlance]. <br> |
- | </td></tr> | + | </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=2m6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m6s OCA], [https://pdbe.org/2m6s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m6s RCSB], [https://www.ebi.ac.uk/pdbsum/2m6s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m6s ProSAT]</span></td></tr> |
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- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2m6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m6s OCA], [https://pdbe.org/2m6s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m6s RCSB], [https://www.ebi.ac.uk/pdbsum/2m6s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m6s ProSAT]</span></td></tr> | + | |
</table> | </table> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Flavodoxins are a family of FMN binding proteins widely distributed in prokaryotes. They involve in various electron transfer reactions using the non-covalently bound FMN cofactor as the redox center. The Escherichia coli yqcA gene was identified to encode a short-chain favodoxin based on sequence information. However, the structure of YqcA protein is unknown and its exact biological function in cell is yet to be investigated. Herein, we report the resonance assignments of 1H, 13C and 15N atoms of E. coli YqcA in both the apo and holo states. | ||
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- | H, C and N resonance assignments of the apo and holo states of flavodoxin YqcA from Escherichia coli.,Ye Q, Hu Y, Jin C Biomol NMR Assign. 2013 Jun 9. PMID:23749454<ref>PMID:23749454</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 2m6s" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Flavodoxin 3D structures|Flavodoxin 3D structures]] | *[[Flavodoxin 3D structures|Flavodoxin 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Hu | + | [[Category: Hu Y]] |
- | [[Category: Jin | + | [[Category: Jin C]] |
- | [[Category: Ye | + | [[Category: Ye Q]] |
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Revision as of 10:20, 31 August 2022
Holo_YqcA
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Categories: Large Structures | Hu Y | Jin C | Ye Q