2jal

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[[Image:2jal.gif|left|200px]]
 
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{{Structure
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==Beta-glucosidase from Thermotoga maritima in complex with cyclophellitol==
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|PDB= 2jal |SIZE=350|CAPTION= <scene name='initialview01'>2jal</scene>, resolution 1.90&Aring;
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<StructureSection load='2jal' size='340' side='right'caption='[[2jal]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE= <scene name='pdbsite=NUC:Ca+Binding+Site+For+Chain+B'>NUC</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=YLL:(1R,2S,3S,4S,5R,6R)-6-(HYDROXYMETHYL)CYCLOHEXANE-1,2,3,4,5-PENTOL'>YLL</scene>
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<table><tr><td colspan='2'>[[2jal]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JAL FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21]
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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]] 1.9&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=YLL:(1R,2S,3S,4S,5R,6R)-6-(HYDROXYMETHYL)CYCLOHEXANE-1,2,3,4,5-PENTOL'>YLL</scene></td></tr>
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}}
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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=2jal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jal OCA], [https://pdbe.org/2jal PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jal RCSB], [https://www.ebi.ac.uk/pdbsum/2jal PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jal ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BGLA_THEMA BGLA_THEMA]
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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/ja/2jal_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=2jal ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structural basis for beta-glucosidase inhibition by cyclophellitol is demonstrated using X-ray crystallography, enzyme kinetics and mass spectrometry.
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'''BETA-GLUCOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH CYCLOPHELLITOL'''
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Structural basis for cyclophellitol inhibition of a beta-glucosidase.,Gloster TM, Madsen R, Davies GJ Org Biomol Chem. 2007 Feb 7;5(3):444-6. Epub 2006 Dec 14. PMID:17252125<ref>PMID:17252125</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2jal" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The structural basis for beta-glucosidase inhibition by cyclophellitol is demonstrated using X-ray crystallography, enzyme kinetics and mass spectrometry.
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*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2JAL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JAL OCA].
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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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Structural basis for cyclophellitol inhibition of a beta-glucosidase., Gloster TM, Madsen R, Davies GJ, Org Biomol Chem. 2007 Feb 7;5(3):444-6. Epub 2006 Dec 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17252125 17252125]
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[[Category: Beta-glucosidase]]
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[[Category: Single protein]]
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Davies, G J.]]
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[[Category: Davies GJ]]
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[[Category: Gloster, T M.]]
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[[Category: Gloster TM]]
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[[Category: Madsen, R.]]
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[[Category: Madsen R]]
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[[Category: ACT]]
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[[Category: CA]]
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[[Category: YLL]]
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[[Category: carbohydrate metabolism]]
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[[Category: cellulose degradation]]
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[[Category: covalent]]
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[[Category: family 1]]
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[[Category: glycosidase]]
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[[Category: glycoside hydrolase]]
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[[Category: hydrolase]]
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[[Category: inhibitor]]
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[[Category: polysaccharide degradation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:39:25 2008''
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Current revision

Beta-glucosidase from Thermotoga maritima in complex with cyclophellitol

PDB ID 2jal

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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