3e67: Difference between revisions

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[[Image:3e67.png|left|200px]]


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==Murine inos dimer with inhibitor 4-MAP bound==
The line below this paragraph, containing "STRUCTURE_3e67", creates the "Structure Box" on the page.
<StructureSection load='3e67' size='340' side='right'caption='[[3e67]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3e67]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E67 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#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=BVF:4-METHYLPYRIDIN-2-AMINE'>BVF</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
{{STRUCTURE_3e67|  PDB=3e67  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e67 OCA], [https://pdbe.org/3e67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e67 RCSB], [https://www.ebi.ac.uk/pdbsum/3e67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e67 ProSAT]</span></td></tr>
 
</table>
===Murine inos dimer with inhibitor 4-MAP bound===
== Function ==
 
[https://www.uniprot.org/uniprot/NOS2_MOUSE NOS2_MOUSE] Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2.<ref>PMID:16373578</ref>
 
== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e6/3e67_consurf.spt"</scriptWhenChecked>
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==About this Structure==
  </jmolCheckbox>
[[3e67]] is a 2 chain structure of [[Nitric Oxide Synthase (Part II)]] and [[Nitric oxide synthase]] with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E67 OCA].  
</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=3e67 ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Nitric Oxide Synthase (Part II)]]
*[[Nitric Oxide Synthase 3D structures|Nitric Oxide Synthase 3D structures]]
*[[Nitric oxide synthase]]
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:018849972</ref><references group="xtra"/>
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Nitric-oxide synthase]]
[[Category: Aberg A]]
[[Category: Aberg, A.]]
[[Category: Andersson G]]
[[Category: Andersson, G.]]
[[Category: Andrews G]]
[[Category: Andrews, G.]]
[[Category: Arvai AS]]
[[Category: Arvai, A S.]]
[[Category: Cheshire DR]]
[[Category: Cheshire, D R.]]
[[Category: Connolly S]]
[[Category: Connolly, S.]]
[[Category: Crane BR]]
[[Category: Crane, B R.]]
[[Category: Garcin ED]]
[[Category: Garcin, E D.]]
[[Category: Gensmantel NP]]
[[Category: Gensmantel, N P.]]
[[Category: Getzoff ED]]
[[Category: Getzoff, E D.]]
[[Category: Hamley PJ]]
[[Category: Hamley, P J.]]
[[Category: Kroeger MD]]
[[Category: Kroeger, M D.]]
[[Category: Mallinder PR]]
[[Category: Mallinder, P R.]]
[[Category: Mete A]]
[[Category: Mete, A.]]
[[Category: Nicholls DJ]]
[[Category: Nicholls, D J.]]
[[Category: Rosenfeld RJ]]
[[Category: Rosenfeld, R J.]]
[[Category: St-Gallay SA]]
[[Category: St-Gallay, S A.]]
[[Category: Stueh DJ]]
[[Category: Stueh, D J.]]
[[Category: Tainer JA]]
[[Category: Tainer, J A.]]
[[Category: Tinker AC]]
[[Category: Tinker, A C.]]
[[Category: Wallace AV]]
[[Category: Wallace, A V.]]
[[Category: Calmodulin-binding]]
[[Category: Dimer]]
[[Category: Fad]]
[[Category: Fmn]]
[[Category: Heme]]
[[Category: Iron]]
[[Category: Isozyme-specific inhibitor]]
[[Category: Metal-binding]]
[[Category: Nadp]]
[[Category: Nitric oxide sythase]]
[[Category: Oxidoreductase]]
[[Category: Oxygenase domain]]

Latest revision as of 12:44, 21 February 2024

Murine inos dimer with inhibitor 4-MAP boundMurine inos dimer with inhibitor 4-MAP bound

Structural highlights

3e67 is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NOS2_MOUSE Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Kim SF, Huri DA, Snyder SH. Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2. Science. 2005 Dec 23;310(5756):1966-70. PMID:16373578 doi:http://dx.doi.org/10.1126/science.1119407

3e67, resolution 2.60Å

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OCA