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1ave

From Proteopedia

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{{Seed}}
 
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[[Image:1ave.png|left|200px]]
 
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==CRYSTAL STRUCTURE OF HEN EGG-WHITE APO-AVIDIN IN RELATION TO ITS THERMAL STABILITY PROPERTIES==
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The line below this paragraph, containing "STRUCTURE_1ave", creates the "Structure Box" on the page.
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<StructureSection load='1ave' size='340' side='right'caption='[[1ave]], [[Resolution|resolution]] 2.80&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'>[[1ave]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AVE 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]] 2.8&#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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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{{STRUCTURE_1ave| PDB=1ave | 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=1ave FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ave OCA], [https://pdbe.org/1ave PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ave RCSB], [https://www.ebi.ac.uk/pdbsum/1ave PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ave ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AVID_CHICK AVID_CHICK] The biological function of avidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of avidin).
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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/av/1ave_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=1ave ConSurf].
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<div style="clear:both"></div>
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===CRYSTAL STRUCTURE OF HEN EGG-WHITE APO-AVIDIN IN RELATION TO ITS THERMAL STABILITY PROPERTIES===
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==See Also==
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*[[Avidin 3D structures|Avidin 3D structures]]
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__TOC__
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</StructureSection>
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The line below this paragraph, {{ABSTRACT_PUBMED_8289264}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 8289264 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8289264}}
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==About this Structure==
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1AVE is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVE OCA].
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==Reference==
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<ref group="xtra">PMID:8289264</ref><references group="xtra"/>
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Bolognesi, M.]]
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[[Category: Large Structures]]
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[[Category: Coda, A.]]
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[[Category: Bolognesi M]]
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[[Category: Malcovati, M.]]
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[[Category: Coda A]]
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[[Category: Pugliese, L.]]
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[[Category: Malcovati M]]
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[[Category: Biotin-binding protein]]
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[[Category: Pugliese L]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:45:33 2009''
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Current revision

CRYSTAL STRUCTURE OF HEN EGG-WHITE APO-AVIDIN IN RELATION TO ITS THERMAL STABILITY PROPERTIES

PDB ID 1ave

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