2taa

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{{Seed}}
 
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[[Image:2taa.png|left|200px]]
 
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==STRUCTURE AND POSSIBLE CATALYTIC RESIDUES OF TAKA-AMYLASE A==
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The line below this paragraph, containing "STRUCTURE_2taa", creates the "Structure Box" on the page.
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<StructureSection load='2taa' size='340' side='right'caption='[[2taa]], [[Resolution|resolution]] 3.00&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'>[[2taa]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1taa 1taa]. The February 2006 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Alpha-amylase'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2006_2 10.2210/rcsb_pdb/mom_2006_2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2TAA 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]] 3&#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=CA:CALCIUM+ION'>CA</scene></td></tr>
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{{STRUCTURE_2taa| PDB=2taa | 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=2taa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2taa OCA], [https://pdbe.org/2taa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2taa RCSB], [https://www.ebi.ac.uk/pdbsum/2taa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2taa ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMYA1_ASPOR AMYA1_ASPOR]
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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/ta/2taa_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=2taa 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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A complete molecular model of Taka-amylase A consisting of 478 amino acid residues was built with the aid of amino acid sequence data. Some typical structural features of the molecule are described. A model fitting of an amylose chain in the catalytic site of the enzyme showed a possible productive binding mode between substrate and enzyme. On the basis of the difference Fourier analysis and the model fitting study, glutamic acid (Glu230) and aspartic acid (Asp297), which are located at the bottom of the cleft, were concluded to be the catalytic residues, serving as the general acid and base, respectively.
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===STRUCTURE AND POSSIBLE CATALYTIC RESIDUES OF TAKA-AMYLASE A===
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Structure and possible catalytic residues of Taka-amylase A.,Matsuura Y, Kusunoki M, Harada W, Kakudo M J Biochem. 1984 Mar;95(3):697-702. PMID:6609921<ref>PMID:6609921</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 2taa" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_6609921}}, adds the Publication Abstract to the page
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*[[Amylase 3D structures|Amylase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 6609921 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_6609921}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2TAA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1taa 1taa]. Additional information on 2TAA is available in a page on [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb74_1.html Alpha Amylase] at the RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TAA OCA].
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==Reference==
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Structure and possible catalytic residues of Taka-amylase A., Matsuura Y, Kusunoki M, Harada W, Kakudo M, J Biochem. 1984 Mar;95(3):697-702. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/6609921 6609921]
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[[Category: Alpha Amylase]]
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[[Category: Alpha-amylase]]
[[Category: Alpha-amylase]]
[[Category: Aspergillus oryzae]]
[[Category: Aspergillus oryzae]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kakudo, M.]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Kusunoki, M.]]
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[[Category: Kakudo M]]
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[[Category: Matsuura, Y.]]
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[[Category: Kusunoki M]]
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[[Category: Tanaka, N.]]
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[[Category: Matsuura Y]]
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[[Category: Tanaka N]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 23 10:54:33 2008''
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Current revision

STRUCTURE AND POSSIBLE CATALYTIC RESIDUES OF TAKA-AMYLASE A

PDB ID 2taa

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