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New page: left|200px<br /><applet load="1ndh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ndh, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1ndh.jpg|left|200px]]<br /><applet load="1ndh" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ndh, resolution 2.1&Aring;" />
'''CRYSTAL STRUCTURE OF NADH-CYTOCHROME B5 REDUCTASE FROM PIG LIVER AT 2.4 ANGSTROMS RESOLUTION'''<br />


==Overview==
==CRYSTAL STRUCTURE OF NADH-CYTOCHROME B5 REDUCTASE FROM PIG LIVER AT 2.4 ANGSTROMS RESOLUTION==
The three-dimensional structure of NADH-cytochrome b5 reductase from pig, liver microsomes has been determined at 2.4 A resolution by X-ray, crystallography. The molecular structure reveals two domains, the FAD, binding domain and the NADH domain. A large cleft lies between these two, domains and contains the binding site for the FAD prosthetic group. The, backbone structure of the FAD binding domain has a great similarity to, that of ferredoxin-NADP+ reductase [Karplus, P. A., Daniels, M. J., &amp;, Herriott, J. R. (1991) Science 251, 60-65], in spite of the relatively low, sequence homology (about 15%) between the two enzymes. On the other hand, the structure of the NADH domain has several structural differences from, that of the NADP+ domain of ferredoxin-NADP+ reductase. The size of the, cleft between the two domains is larger in NADH-cytochrome b5 reductase, than in ferredoxin-NADP+ reductase, which may be responsible for the, observed difference in the nucleotide accessibility in the two enzymes.
<StructureSection load='1ndh' size='340' side='right'caption='[[1ndh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ndh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NDH 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]] 2.1&#8491;</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></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=1ndh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ndh OCA], [https://pdbe.org/1ndh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ndh RCSB], [https://www.ebi.ac.uk/pdbsum/1ndh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ndh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NB5R3_PIG NB5R3_PIG] Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.[:]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nd/1ndh_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ndh ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1NDH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with FAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NDH OCA].
*[[NADH-cytochrome b5 reductase|NADH-cytochrome b5 reductase]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution., Nishida H, Inaka K, Yamanaka M, Kaida S, Kobayashi K, Miki K, Biochemistry. 1995 Mar 7;34(9):2763-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7893687 7893687]
[[Category: Large Structures]]
[[Category: Cytochrome-b5 reductase]]
[[Category: Single protein]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Miki, K.]]
[[Category: Miki K]]
[[Category: Nishida, H.]]
[[Category: Nishida H]]
[[Category: FAD]]
[[Category: electron transport (flavo protein)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:09:45 2007''

Latest revision as of 07:55, 14 February 2024

CRYSTAL STRUCTURE OF NADH-CYTOCHROME B5 REDUCTASE FROM PIG LIVER AT 2.4 ANGSTROMS RESOLUTION

1ndh, resolution 2.10Å

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