1bc2: Difference between revisions

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[[Image:1bc2.png|left|200px]]


{{STRUCTURE_1bc2|  PDB=1bc2  |  SCENE=  }}
==ZN-DEPENDENT METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS==
 
<StructureSection load='1bc2' size='340' side='right'caption='[[1bc2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
===ZN-DEPENDENT METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS===
== 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>
{{ABSTRACT_PUBMED_9730812}}
</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>
==About this Structure==
<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>
[[1bc2]] is a 2 chain structure of [[Beta-lactamase]] with sequence from [http://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].  
</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>


==See Also==
==See Also==
*[[Beta-lactamase|Beta-lactamase]]
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:009730812</ref><ref group="xtra">PMID:010708646</ref><references group="xtra"/>
[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
[[Category: Beta-lactamase]]
[[Category: Large Structures]]
[[Category: Fabiane, S M.]]
[[Category: Fabiane SM]]
[[Category: Sutton, B J.]]
[[Category: Sutton BJ]]
[[Category: Antibiotic resistance]]
[[Category: Hydrolase]]
[[Category: Metallo beta-lactamase]]
[[Category: Penicillinase]]

Latest revision as of 09:35, 7 February 2024

ZN-DEPENDENT METALLO-BETA-LACTAMASE FROM BACILLUS CEREUSZN-DEPENDENT METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS

Structural highlights

1bc2 is a 2 chain structure with sequence from Bacillus cereus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BLA2_BACCE Can hydrolyze carbapenem compounds.

Evolutionary Conservation

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

See Also

1bc2, resolution 1.90Å

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