1cpy: Difference between revisions

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New page: left|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 2.6&Aring;" />
'''SITE-DIRECTED MUTAGENESIS ON (SERINE) CARBOXYPEPTIDASE Y FROM YEAST. THE SIGNIFICANCE OF THR 60 AND MET 398 IN HYDROLYSIS AND AMINOLYSIS REACTIONS'''<br />


==About this Structure==
==SITE-DIRECTED MUTAGENESIS ON (SERINE) CARBOXYPEPTIDASE Y FROM YEAST. THE SIGNIFICANCE OF THR 60 AND MET 398 IN HYDROLYSIS AND AMINOLYSIS REACTIONS==
1CPY 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 NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Carboxypeptidase_C Carboxypeptidase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.5 3.4.16.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CPY OCA].  
<StructureSection load='1cpy' size='340' side='right'caption='[[1cpy]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
[[Category: Carboxypeptidase C]]
== 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]] 2.6&#8491;</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: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Breddam K]]
[[Category: Breddam, K.]]
[[Category: Mortensen U]]
[[Category: Mortensen, U.]]
[[Category: Raaschou-Nielsen M]]
[[Category: Raaschou-Nielsen, M.]]
[[Category: Remington SJ]]
[[Category: Remington, S.J.]]
[[Category: Sorensen SB]]
[[Category: Sorensen, S.B.]]
[[Category: NAG]]
[[Category: hydrolase (carboxypeptidase)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:39:50 2007''

Latest revision as of 07:26, 17 October 2024

SITE-DIRECTED MUTAGENESIS ON (SERINE) CARBOXYPEPTIDASE Y FROM YEAST. THE SIGNIFICANCE OF THR 60 AND MET 398 IN HYDROLYSIS AND AMINOLYSIS REACTIONSSITE-DIRECTED MUTAGENESIS ON (SERINE) CARBOXYPEPTIDASE Y FROM YEAST. THE SIGNIFICANCE OF THR 60 AND MET 398 IN HYDROLYSIS AND AMINOLYSIS REACTIONS

Structural highlights

1cpy is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

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

See Also

1cpy, resolution 2.60Å

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