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3eqa

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[[Image:3eqa.png|left|200px]]
 
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==Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol==
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The line below this paragraph, containing "STRUCTURE_3eqa", creates the "Structure Box" on the page.
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<StructureSection load='3eqa' size='340' side='right'caption='[[3eqa]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3eqa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EQA FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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{{STRUCTURE_3eqa| PDB=3eqa | SCENE= }}
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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=3eqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eqa OCA], [https://pdbe.org/3eqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eqa RCSB], [https://www.ebi.ac.uk/pdbsum/3eqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eqa ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMYG_ASPNG AMYG_ASPNG]
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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/eq/3eqa_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=3eqa 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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Glucoamylase from Aspergillus niger is an industrially important biocatalyst that is utilized in the mass production of glucose from raw starch or soluble oligosaccharides. The G1 isoform consists of a catalytic domain and a starch-binding domain connected by a heavily glycosylated linker region. The amino-terminal catalytic domain of the G1 isoform generated by subtilisin cleavage has been crystallized at pH 8.5, which is a significantly higher pH condition than used for previously characterized glucoamylase crystals. The refined structure at 1.9 A resolution reveals the active site of the enzyme in complex with both Tris and glycerol molecules. The ligands display both unique and analogous interactions with the substrate-binding site when compared with previous structures of homologous enzymes bound to inhibitors.
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===Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol===
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Structure of the catalytic domain of glucoamylase from Aspergillus niger.,Lee J, Paetzel M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Feb 1;67(Pt, 2):188-92. Epub 2011 Jan 21. PMID:21301084<ref>PMID:21301084</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 3eqa" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_21301084}}, adds the Publication Abstract to the page
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*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 21301084 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_21301084}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[3eqa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EQA OCA].
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==Reference==
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<ref group="xtra">PMID:21301084</ref><references group="xtra"/>
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[[Category: Aspergillus niger]]
[[Category: Aspergillus niger]]
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[[Category: Glucan 1,4-alpha-glucosidase]]
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[[Category: Large Structures]]
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[[Category: Lee, J.]]
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[[Category: Lee J]]
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[[Category: Paetzel, M.]]
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[[Category: Paetzel M]]

Current revision

Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol

PDB ID 3eqa

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