3eah: Difference between revisions

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[[Image:3eah.png|left|200px]]


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==Structure of inhibited human eNOS oxygenase domain==
The line below this paragraph, containing "STRUCTURE_3eah", creates the "Structure Box" on the page.
<StructureSection load='3eah' size='340' side='right'caption='[[3eah]], [[Resolution|resolution]] 2.44&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3eah]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EAH FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.44&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=327:(3S,5E)-3-PROPYL-3,4-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-5(2H)-IMINE'>327</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_3eah| PDB=3eah |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eah OCA], [https://pdbe.org/3eah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eah RCSB], [https://www.ebi.ac.uk/pdbsum/3eah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eah ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NOS3_HUMAN NOS3_HUMAN] Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.<ref>PMID:17264164</ref>  Isoform eNOS13C: Lacks eNOS activity, dominant-negative form that may down-regulate eNOS activity by forming heterodimers with isoform 1.<ref>PMID:17264164</ref>
== 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/ea/3eah_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=3eah ConSurf].
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===Structure of inhibited human eNOS oxygenase domain===
==See Also==
 
*[[Nitric Oxide Synthase 3D structures|Nitric Oxide Synthase 3D structures]]
 
== References ==
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{{ABSTRACT_PUBMED_18849972}}
 
==About this Structure==
3EAH is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAH OCA].
 
==Reference==
<ref group="xtra">PMID:18849972</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Nitric-oxide synthase]]
[[Category: Large Structures]]
[[Category: Aberg, A.]]
[[Category: Aberg A]]
[[Category: Andersson, G.]]
[[Category: Andersson G]]
[[Category: Andrews, G.]]
[[Category: Andrews G]]
[[Category: Arvai, A S.]]
[[Category: Arvai AS]]
[[Category: Cheshire, D R.]]
[[Category: Cheshire DR]]
[[Category: Connolly, S.]]
[[Category: Connolly S]]
[[Category: Crane, B R.]]
[[Category: Crane BR]]
[[Category: Garcin, E D.]]
[[Category: Garcin ED]]
[[Category: Gensmantel, N P.]]
[[Category: Gensmantel NP]]
[[Category: Getzoff, E D.]]
[[Category: Getzoff ED]]
[[Category: Hamley, P J.]]
[[Category: Hamley PJ]]
[[Category: Kroeger, M D.]]
[[Category: Kroeger MD]]
[[Category: Mallinder, P R.]]
[[Category: Mallinder PR]]
[[Category: Mete, A.]]
[[Category: Mete A]]
[[Category: Nicholls, D J.]]
[[Category: Nicholls DJ]]
[[Category: Rosenfeld, R J.]]
[[Category: Rosenfeld RJ]]
[[Category: St-Gallay, S A.]]
[[Category: St-Gallay SA]]
[[Category: Stuehr, D J.]]
[[Category: Stuehr DJ]]
[[Category: Tainer, J A.]]
[[Category: Tainer JA]]
[[Category: Tinker, A C.]]
[[Category: Tinker AC]]
[[Category: Wallace, A V.]]
[[Category: Wallace AV]]
[[Category: Fad]]
[[Category: Fmn]]
[[Category: Heme]]
[[Category: Iron]]
[[Category: Metal-binding]]
[[Category: Nadp]]
[[Category: Nitric oxide synthase]]
[[Category: No]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase calmodulin-binding]]
[[Category: Polymorphism]]
[[Category: Tetrahydrobiopterin]]
[[Category: Zinc]]
 
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