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1yma

From Proteopedia

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{{Seed}}
 
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[[Image:1yma.png|left|200px]]
 
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==STRUCTURAL CHARACTERIZATION OF HEME LIGATION IN THE HIS64-->TYR VARIANT OF MYOGLOBIN==
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The line below this paragraph, containing "STRUCTURE_1yma", creates the "Structure Box" on the page.
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<StructureSection load='1yma' size='340' side='right'caption='[[1yma]], [[Resolution|resolution]] 2.00&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'>[[1yma]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YMA 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]] 2&#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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1yma| PDB=1yma | 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=1yma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yma OCA], [https://pdbe.org/1yma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yma RCSB], [https://www.ebi.ac.uk/pdbsum/1yma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yma ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE] 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/ym/1yma_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=1yma ConSurf].
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<div style="clear:both"></div>
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===STRUCTURAL CHARACTERIZATION OF HEME LIGATION IN THE HIS64-->TYR VARIANT OF MYOGLOBIN===
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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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</StructureSection>
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The line below this paragraph, {{ABSTRACT_PUBMED_8175669}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 8175669 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8175669}}
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==About this Structure==
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1YMA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YMA OCA].
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==Reference==
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Structural characterization of heme ligation in the His64--&gt;Tyr variant of myoglobin., Maurus R, Bogumil R, Luo Y, Tang HL, Smith M, Mauk AG, Brayer GD, J Biol Chem. 1994 Apr 29;269(17):12606-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8175669 8175669]
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[[Category: Equus caballus]]
[[Category: Equus caballus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Brayer, G D.]]
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[[Category: Brayer GD]]
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[[Category: Maurus, R.]]
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[[Category: Maurus R]]
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[[Category: Oxygen transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:04:29 2008''
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Current revision

STRUCTURAL CHARACTERIZATION OF HEME LIGATION IN THE HIS64-->TYR VARIANT OF MYOGLOBIN

PDB ID 1yma

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