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1bep

From Proteopedia

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[[Image:1bep.jpg|left|200px]]<br /><applet load="1bep" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bep, resolution 2.2&Aring;" />
 
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'''EFFECT OF UNNATURAL HEME SUBSTITUTION ON KINETICS OF ELECTRON TRANSFER IN CYTOCHROME C PEROXIDASE'''<br />
 
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==About this Structure==
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==EFFECT OF UNNATURAL HEME SUBSTITUTION ON KINETICS OF ELECTRON TRANSFER IN CYTOCHROME C PEROXIDASE==
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1BEP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=CCH:'>CCH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BEP OCA].
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<StructureSection load='1bep' size='340' side='right'caption='[[1bep]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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[[Category: Cytochrome-c peroxidase]]
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== Structural highlights ==
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[[Category: Saccharomyces cerevisiae]]
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<table><tr><td colspan='2'>[[1bep]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BEP FirstGlance]. <br>
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[[Category: Single protein]]
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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]] 2.2&#8491;</td></tr>
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[[Category: Kraut, J.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CCH:[7-ETHENYL-12-FORMYL-3,8,13,17-TERTRAMETHYL-21H,23H-PORPHINE-2,18-DIPROPANOATO(2)-N21,N22,N23,N24]IRON'>CCH</scene></td></tr>
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[[Category: Miller, M.]]
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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=1bep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bep OCA], [https://pdbe.org/1bep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bep RCSB], [https://www.ebi.ac.uk/pdbsum/1bep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bep ProSAT]</span></td></tr>
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[[Category: CCH]]
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</table>
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[[Category: oxidoreductase]]
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== Function ==
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[[Category: peroxidase]]
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[https://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
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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/be/1bep_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=1bep ConSurf].
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<div style="clear:both"></div>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:34 2008''
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==See Also==
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*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Kraut J]]
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[[Category: Miller M]]

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EFFECT OF UNNATURAL HEME SUBSTITUTION ON KINETICS OF ELECTRON TRANSFER IN CYTOCHROME C PEROXIDASE

PDB ID 1bep

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