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5mba

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[[Image:5mba.gif|left|200px]]<br /><applet load="5mba" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="5mba, resolution 1.9&Aring;" />
 
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'''BINDING MODE OF AZIDE TO FERRIC APLYSIA LIMACINA MYOGLOBIN. CRYSTALLOGRAPHIC ANALYSIS AT 1.9 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==BINDING MODE OF AZIDE TO FERRIC APLYSIA LIMACINA MYOGLOBIN. CRYSTALLOGRAPHIC ANALYSIS AT 1.9 ANGSTROMS RESOLUTION==
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<StructureSection load='5mba' size='340' side='right'caption='[[5mba]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5mba]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aplli Aplli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2mba 2mba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MBA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MBA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5mba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mba OCA], [http://pdbe.org/5mba PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mba RCSB], [http://www.ebi.ac.uk/pdbsum/5mba PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mba ProSAT]</span></td></tr>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mb/5mba_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=5mba ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
The binding mode of azide to the ferric form of Aplysia limacina myoglobin has been studied by X-ray crystallography. The three-dimensional structure of the complex has been refined at 1.9 A resolution to a crystallographic R-factor of 13.9%, including 126 ordered solvent molecules. Azide binds to the heme iron, at the sixth co-ordination position, and is oriented towards the outer part of the distal site crevice. This orientation is stabilized by an ionic interaction with the side-chain of Arg66 (E10) which, from an outer orientation in the 'aquo-met' ligand-free myoglobin, folds back towards the distal site in the presence of the anionic ligand. In the absence of a hydrogen bond donor residue at the distal E7 position in Aplysia limacina myoglobin, a different polar residue, Arg66 at the E10 topological position, has been selected by molecular evolution in order to grant ligand stabilization.
The binding mode of azide to the ferric form of Aplysia limacina myoglobin has been studied by X-ray crystallography. The three-dimensional structure of the complex has been refined at 1.9 A resolution to a crystallographic R-factor of 13.9%, including 126 ordered solvent molecules. Azide binds to the heme iron, at the sixth co-ordination position, and is oriented towards the outer part of the distal site crevice. This orientation is stabilized by an ionic interaction with the side-chain of Arg66 (E10) which, from an outer orientation in the 'aquo-met' ligand-free myoglobin, folds back towards the distal site in the presence of the anionic ligand. In the absence of a hydrogen bond donor residue at the distal E7 position in Aplysia limacina myoglobin, a different polar residue, Arg66 at the E10 topological position, has been selected by molecular evolution in order to grant ligand stabilization.
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==About this Structure==
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Binding mode of azide to ferric Aplysia limacina myoglobin. Crystallographic analysis at 1.9 A resolution.,Mattevi A, Gatti G, Coda A, Rizzi M, Ascenzi P, Brunori M, Bolognesi M J Mol Recognit. 1991 Feb;4(1):1-6. PMID:1931125<ref>PMID:1931125</ref>
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5MBA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_limacina Aplysia limacina] with <scene name='pdbligand=AZI:'>AZI</scene>, <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 2MBA. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MBA OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Binding mode of azide to ferric Aplysia limacina myoglobin. Crystallographic analysis at 1.9 A resolution., Mattevi A, Gatti G, Coda A, Rizzi M, Ascenzi P, Brunori M, Bolognesi M, J Mol Recognit. 1991 Feb;4(1):1-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1931125 1931125]
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</div>
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[[Category: Aplysia limacina]]
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<div class="pdbe-citations 5mba" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Ascenzi, P.]]
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[[Category: Bolognesi, M.]]
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[[Category: Brunori, M.]]
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[[Category: Coda, A.]]
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[[Category: Gatti, G.]]
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[[Category: Onesti, S.]]
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[[Category: ACE]]
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[[Category: AZI]]
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[[Category: HEM]]
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[[Category: oxygen storage]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:15:30 2008''
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==See Also==
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*[[Myoglobin 3D structures|Myoglobin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Aplli]]
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[[Category: Large Structures]]
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[[Category: Ascenzi, P]]
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[[Category: Bolognesi, M]]
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[[Category: Brunori, M]]
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[[Category: Coda, A]]
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[[Category: Gatti, G]]
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[[Category: Onesti, S]]
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[[Category: Oxygen storage]]

Current revision

BINDING MODE OF AZIDE TO FERRIC APLYSIA LIMACINA MYOGLOBIN. CRYSTALLOGRAPHIC ANALYSIS AT 1.9 ANGSTROMS RESOLUTION

PDB ID 5mba

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