1bvc

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[[Image:1bvc.gif|left|200px]]
 
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==STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM D) AT 118 K==
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The line below this paragraph, containing "STRUCTURE_1bvc", creates the "Structure Box" on the page.
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<StructureSection load='1bvc' size='340' side='right'caption='[[1bvc]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1bvc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BVC FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.5&#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=BLA:BILIVERDINE+IX+ALPHA'>BLA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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{{STRUCTURE_1bvc| PDB=1bvc | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bvc OCA], [https://pdbe.org/1bvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bvc RCSB], [https://www.ebi.ac.uk/pdbsum/1bvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bvc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
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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/bv/1bvc_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=1bvc ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM D) AT 118 K'''
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==See Also==
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*[[Myoglobin 3D structures|Myoglobin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Crystal structure determinations of two orthorhombic (P2(1)2(1)2(1)) crystal modifications of the biliverdin apomyoglobin complex are described. The two structures were determined by X-ray diffraction at 100 K to a resolution of 1.5 A and 1.4 A. Both crystal forms were grown by hanging-drop techniques, using phosphate as precipitant. The structures were solved by molecular replacement and refined to final R-values of 19.4% and 21.2%. Both structures are very similar with respect to the binding site and the conformation of the biliverdin chromophore, which occurs in a (P) helical conformation. It is located within the heme pocket, very close in position and orientation to the heme binding site in myoglobin. Two water molecules not present in the crystal structure of myoglobin are sequestered within the heme pocket in the biliverdin-apomyoglobin complex, and they are engaged in hydrogen bonding to the biliverdin and to the protein. Comparison with structural results from an earlier NMR study of the same complex shows good agreement.
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[[Category: Large Structures]]
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==About this Structure==
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1BVC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BVC OCA].
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==Reference==
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Structure determination of the biliverdin apomyoglobin complex: crystal structure analysis of two crystal forms at 1.4 and 1.5 A resolution., Wagner UG, Muller N, Schmitzberger W, Falk H, Kratky C, J Mol Biol. 1995 Mar 24;247(2):326-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7707378 7707378]
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[[Category: Physeter catodon]]
[[Category: Physeter catodon]]
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[[Category: Single protein]]
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[[Category: Falk H]]
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[[Category: Falk, H.]]
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[[Category: Kratky C]]
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[[Category: Kratky, C.]]
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[[Category: Mueller N]]
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[[Category: Mueller, N.]]
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[[Category: Schmitzberger W]]
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[[Category: Schmitzberger, W.]]
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[[Category: Wagner UG]]
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[[Category: Wagner, U G.]]
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[[Category: Oxygen storage]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:59:47 2008''
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Current revision

STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM D) AT 118 K

PDB ID 1bvc

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