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1lbs

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[[Image:1lbs.jpg|left|200px]]<br /><applet load="1lbs" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lbs, resolution 2.6&Aring;" />
 
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'''LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)'''<br />
 
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==Overview==
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==LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)==
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Many lipases are potent catalysts of stereoselective reactions and are therefore of interest for use in chemical synthesis. The crystal structures of lipases show a large variation in the shapes of their active site environments that may explain the large variation in substrate specificity of these enzymes. We have determined the three-dimensional structure of Candida antarctica lipase B (CALB) cocrystallized with the detergent Tween 80. In another crystal form, the structure of the enzyme in complex with a covalently bound phosphonate inhibitor has been determined. In both structures, the active site is exposed to the external solvent. The potential lid-forming helix alpha 5 in CALB is well-ordered in the Tween 80 structure and disordered in the inhibitor complex. The tetrahedral intermediates of two chiral substrates have been modeled on the basis of available structural and biochemical information. The results of this study provide a structural explanation for the high stereoselectivity of CALB toward many secondary alcohols.
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<StructureSection load='1lbs' size='340' side='right'caption='[[1lbs]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1lbs]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Moesziomyces_antarcticus Moesziomyces antarcticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LBS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LBS FirstGlance]. <br>
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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]] 2.6&#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=HEE:N-HEXYLPHOSPHONATE+ETHYL+ESTER'>HEE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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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=1lbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lbs OCA], [https://pdbe.org/1lbs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lbs RCSB], [https://www.ebi.ac.uk/pdbsum/1lbs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lbs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LIPB_PSEA2 LIPB_PSEA2] Hydrolysis of triglycerides. Is very stereospecific both in hydrolysis and in organic synthesis and has a potentially important application in glucolipid synthesis.
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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/1lbs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1lbs ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1LBS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_antarctica Candida antarctica] with <scene name='pdbligand=HEE:'>HEE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LBS OCA].
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols., Uppenberg J, Ohrner N, Norin M, Hult K, Kleywegt GJ, Patkar S, Waagen V, Anthonsen T, Jones TA, Biochemistry. 1995 Dec 26;34(51):16838-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8527460 8527460]
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[[Category: Large Structures]]
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[[Category: Candida antarctica]]
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[[Category: Moesziomyces antarcticus]]
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[[Category: Single protein]]
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[[Category: Jones TA]]
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[[Category: Triacylglycerol lipase]]
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[[Category: Uppenberg J]]
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[[Category: Jones, T A.]]
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[[Category: Uppenberg, J.]]
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[[Category: HEE]]
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[[Category: hydrolase (carboxylic esterase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:28 2008''
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Current revision

LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)

PDB ID 1lbs

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