View source for 5gv8


==Structure of NADH-cytochrome b5 reductase refined with the multipolar atomic model at 0.78A==
<StructureSection load='5gv8' size='340' side='right'caption='[[5gv8]], [[Resolution|resolution]] 0.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5gv8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GV8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GV8 FirstGlance]. <br>
</td></tr><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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gv7|5gv7]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-b5_reductase Cytochrome-b5 reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.2.2 1.6.2.2] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5gv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gv8 OCA], [http://pdbe.org/5gv8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gv8 RCSB], [http://www.ebi.ac.uk/pdbsum/5gv8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gv8 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/NB5R3_PIG NB5R3_PIG]] Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.[:] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Flavin compounds such as flavin adenine dinucleotide (FAD), flavin mononucleotide and riboflavin make up the active centers in flavoproteins that facilitate various oxidoreductive processes. The fine structural features of the hydrogens and valence electrons of the flavin molecules in the protein environment are critical to the functions of the flavoproteins. However, information on these features cannot be obtained from conventional protein X-ray analyses at ordinary resolution. Here we report the charge density analysis of a flavoenzyme, NADH-cytochrome b5 reductase (b5R), at an ultra-high resolution of 0.78 A. Valence electrons on the FAD cofactor as well as the peptide portion, which are clearly visualized even after the conventional refinement, are analyzed by the multipolar atomic model refinement. The topological analysis for the determined electron density reveals the valence electronic structure of the isoalloxazine ring of FAD and hydrogen-bonding interactions with the protein environment. The tetrahedral electronic distribution around the N5 atom of FAD in b5R is stabilized by hydrogen bonding with CalphaH of Tyr65 and amide-H of Thr66. The hydrogen bonding network leads to His49 composing the cytochrome b5-binding site via non-classical hydrogen bonds between N5 of FAD and CalphaH of Tyr65 and O of Tyr65 and CbetaH of His49.

Distribution of valence electrons of the flavin cofactor in NADH-cytochrome b5 reductase.,Takaba K, Takeda K, Kosugi M, Tamada T, Miki K Sci Rep. 2017 Feb 22;7:43162. doi: 10.1038/srep43162. PMID:28225078<ref>PMID:28225078</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5gv8" style="background-color:#fffaf0;"></div>

==See Also==
*[[NADH-cytochrome b5 reductase|NADH-cytochrome b5 reductase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cytochrome-b5 reductase]]
[[Category: Large Structures]]
[[Category: Miki, K]]
[[Category: Takaba, K]]
[[Category: Takeda, K]]
[[Category: Electron transfer]]
[[Category: Flavoprotein]]
[[Category: Oxidoreductase]]