1bvd: Difference between revisions

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[[Image:1bvd.gif|left|200px]]


{{Structure
==STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM B) AT 98 K==
|PDB= 1bvd |SIZE=350|CAPTION= <scene name='initialview01'>1bvd</scene>, resolution 1.4&Aring;
<StructureSection load='1bvd' size='340' side='right'caption='[[1bvd]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=BLA:BILIVERDINE+IX+ALPHA'>BLA</scene>
<table><tr><td colspan='2'>[[1bvd]] 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=1BVD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BVD FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
|GENE=  
<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></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bvd OCA], [https://pdbe.org/1bvd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bvd RCSB], [https://www.ebi.ac.uk/pdbsum/1bvd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bvd ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bvd OCA], [http://www.ebi.ac.uk/pdbsum/1bvd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bvd RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
== 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/bv/1bvd_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=1bvd ConSurf].
<div style="clear:both"></div>


'''STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM B) AT 98 K'''
==See Also==
 
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
1BVD 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=1BVD OCA].
 
==Reference==
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]
[[Category: Physeter catodon]]
[[Category: Physeter catodon]]
[[Category: Single protein]]
[[Category: Falk H]]
[[Category: Falk, H.]]
[[Category: Kratky C]]
[[Category: Kratky, C.]]
[[Category: Mueller N]]
[[Category: Mueller, N.]]
[[Category: Schmitzberger W]]
[[Category: Schmitzberger, W.]]
[[Category: Wagner UG]]
[[Category: Wagner, U G.]]
[[Category: oxygen storage]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:09:01 2008''

Latest revision as of 09:39, 7 February 2024

STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM B) AT 98 KSTRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM B) AT 98 K

Structural highlights

1bvd is a 1 chain structure with sequence from Physeter catodon. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYG_PHYMC Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.

Evolutionary Conservation

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

See Also

1bvd, resolution 1.40Å

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