1bc2: Difference between revisions

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-[[Image:1bc2.gif|left|200px]]<br />
-<applet load="1bc2" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1bc2, resolution 1.9&Aring;" />
-'''ZN-DEPENDENT METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS'''<br />
-==Overview==
+==ZN-DEPENDENT METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS==
-The structure of the zinc-dependent beta-lactamase II from Bacillus cereus, has been determined at 1.9 A resolution in a crystal form with two, molecules in the asymmetric unit and 400 waters (space group P3121; Rcryst, = 20.8%). The active site contains two zinc ions: Zn1 is tightly, coordinated by His86, His88, and His149, while Zn2 is loosely coordinated, by Asp90, Cys168, and His210. A water molecule (W1) lies between the two, zinc ions but is significantly closer to Zn1 and at a distance of only 1.9, A is effectively a hydroxide moiety and a potential, preactivated, nucleophile. In fact, Asp90 bridges W1 to Zn2, and its location is thus, distinct from that of the bridging water molecules in the binuclear zinc, peptidases or other binuclear zinc hydrolases. Modeling of penicillin, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9730812 (full description)]]
+<StructureSection load='1bc2' size='340' side='right'caption='[[1bc2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1bc2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BC2 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]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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=1bc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bc2 OCA], [https://pdbe.org/1bc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bc2 RCSB], [https://www.ebi.ac.uk/pdbsum/1bc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bc2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/BLA2_BACCE BLA2_BACCE] Can hydrolyze carbapenem compounds.
+== 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/bc/1bc2_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=1bc2 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-BC2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]] with ZN and SO4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BC2 OCA]].
+*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme., Fabiane SM, Sohi MK, Wan T, Payne DJ, Bateson JH, Mitchell T, Sutton BJ, Biochemistry. 1998 Sep 8;37(36):12404-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9730812 9730812]
 [[Category: Bacillus cereus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Fabiane, S.M.]]
+[[Category: Fabiane SM]]
-[[Category: Sutton, B.J.]]
+[[Category: Sutton BJ]]
-[[Category: SO4]]
-[[Category: ZN]]
-[[Category: antibiotic resistance]]
-[[Category: hydrolase]]
-[[Category: metallo beta-lactamase]]
-[[Category: penicillinase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:06:59 2007''