1lbu

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[[Image:1lbu.png|left|200px]]
 
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{{STRUCTURE_1lbu| PDB=1lbu | SCENE= }}
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==HYDROLASE METALLO (ZN) DD-PEPTIDASE==
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<StructureSection load='1lbu' size='340' side='right'caption='[[1lbu]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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===HYDROLASE METALLO (ZN) DD-PEPTIDASE===
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1lbu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_albus_G Streptomyces albus G]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LBU FirstGlance]. <br>
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{{ABSTRACT_PUBMED_011917145}}
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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]] 1.8&#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=ZN:ZINC+ION'>ZN</scene></td></tr>
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==About this Structure==
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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=1lbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lbu OCA], [https://pdbe.org/1lbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lbu RCSB], [https://www.ebi.ac.uk/pdbsum/1lbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lbu ProSAT]</span></td></tr>
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[[1lbu]] is a 1 chain structure of [[Carboxypeptidase]] and [[Penicillin-binding protein]] with sequence from [http://en.wikipedia.org/wiki/Streptomyces_albus Streptomyces albus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LBU OCA].
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CBPM_STRAL CBPM_STRAL] This enzyme catalyzes carboxypeptidation and transpeptidation reactions involved in bacterial cell wall metabolism. It effectively catalyzes the transfer of the N-alpha, N-epsilon-diacetyl-L-lysyl-D-alanyl electrophilic group of the standard tripeptide substrate N-alpha,N-epsilon-diacetyl-L-lysyl-D-alanyl-D-alanine to water. It also performs a weak beta-lactamase activity, hydrolyzing penicillin into penicilloate at a very low rate.
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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/lb/1lbu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1lbu ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
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*[[Carboxypeptidase|Carboxypeptidase]]
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*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
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*[[Penicillin-binding protein|Penicillin-binding protein]]
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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<ref group="xtra">PMID:011917145</ref><references group="xtra"/>
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[[Category: Streptomyces albus G]]
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[[Category: Muramoylpentapeptide carboxypeptidase]]
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[[Category: Charlier P]]
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[[Category: Streptomyces albus]]
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[[Category: Dideberg O]]
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[[Category: Charlier, P.]]
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[[Category: Frere J-M]]
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[[Category: Dideberg, O.]]
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[[Category: Wery J-P]]
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[[Category: Frere, J M.]]
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[[Category: Wery, J P.]]
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[[Category: Carboxypeptidase]]
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[[Category: Hydrolase]]
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[[Category: Nuclear receptor]]
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Current revision

HYDROLASE METALLO (ZN) DD-PEPTIDASE

PDB ID 1lbu

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