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1lbu
From Proteopedia
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| - | [[Image:1lbu.gif|left|200px]]<br /><applet load="1lbu" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1lbu, resolution 1.80Å" /> | ||
| - | '''HYDROLASE METALLO (ZN) DD-PEPTIDASE'''<br /> | ||
| - | == | + | ==HYDROLASE METALLO (ZN) DD-PEPTIDASE== |
| - | + | <StructureSection load='1lbu' size='340' side='right'caption='[[1lbu]], [[Resolution|resolution]] 1.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <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> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | |
| - | + | <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> | |
| - | [ | + | <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> |
| - | + | </table> | |
| - | [[ | + | == Function == |
| - | [ | + | [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. |
| - | [[ | + | == 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/lb/1lbu_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1lbu ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| + | *[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces albus G]] | ||
| + | [[Category: Charlier P]] | ||
| + | [[Category: Dideberg O]] | ||
| + | [[Category: Frere J-M]] | ||
| + | [[Category: Wery J-P]] | ||
Current revision
HYDROLASE METALLO (ZN) DD-PEPTIDASE
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