1cpy
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1cpy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cpy, resolution 2.6Å" /> '''SITE-DIRECTED MUTAGEN...) |
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| - | [[Image:1cpy.jpg|left|200px]]<br /><applet load="1cpy" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1cpy, resolution 2.6Å" /> | ||
| - | '''SITE-DIRECTED MUTAGENESIS ON (SERINE) CARBOXYPEPTIDASE Y FROM YEAST. THE SIGNIFICANCE OF THR 60 AND MET 398 IN HYDROLYSIS AND AMINOLYSIS REACTIONS'''<br /> | ||
| - | == | + | ==SITE-DIRECTED MUTAGENESIS ON (SERINE) CARBOXYPEPTIDASE Y FROM YEAST. THE SIGNIFICANCE OF THR 60 AND MET 398 IN HYDROLYSIS AND AMINOLYSIS REACTIONS== |
| - | + | <StructureSection load='1cpy' size='340' side='right'caption='[[1cpy]], [[Resolution|resolution]] 2.60Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [ | + | <table><tr><td colspan='2'>[[1cpy]] 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=1CPY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CPY FirstGlance]. <br> |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | |
| - | [ | + | <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> |
| - | [ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cpy OCA], [https://pdbe.org/1cpy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cpy RCSB], [https://www.ebi.ac.uk/pdbsum/1cpy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cpy ProSAT]</span></td></tr> |
| - | [[ | + | </table> |
| - | + | == Function == | |
| - | [ | + | [https://www.uniprot.org/uniprot/CBPY_YEAST CBPY_YEAST] Involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate. |
| - | [[ | + | == 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/cp/1cpy_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1cpy ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| + | *[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Breddam K]] | ||
| + | [[Category: Mortensen U]] | ||
| + | [[Category: Raaschou-Nielsen M]] | ||
| + | [[Category: Remington SJ]] | ||
| + | [[Category: Sorensen SB]] | ||
Current revision
SITE-DIRECTED MUTAGENESIS ON (SERINE) CARBOXYPEPTIDASE Y FROM YEAST. THE SIGNIFICANCE OF THR 60 AND MET 398 IN HYDROLYSIS AND AMINOLYSIS REACTIONS
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