1ua3

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[[Image:1ua3.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides==
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|PDB= 1ua3 |SIZE=350|CAPTION= <scene name='initialview01'>1ua3</scene>, resolution 2.01&Aring;
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<StructureSection load='1ua3' size='340' side='right'caption='[[1ua3]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=MLR:MALTOTRIOSE'>MLR</scene>
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<table><tr><td colspan='2'>[[1ua3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UA3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UA3 FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] </span>
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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]] 2.01&#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=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=PRD_900009:alpha-maltotriose'>PRD_900009</scene></td></tr>
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|DOMAIN=
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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=1ua3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ua3 OCA], [https://pdbe.org/1ua3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ua3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ua3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ua3 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1jfh|1JFH]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ua3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ua3 OCA], [http://www.ebi.ac.uk/pdbsum/1ua3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ua3 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/AMYP_PIG AMYP_PIG]
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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/ua/1ua3_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=1ua3 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 X-ray map of a pig pancreatic alpha-amylase crystal soaked (and flash-frozen) with a maltopentaose substrate showed a pattern of electron density corresponding to the binding of oligosaccharides at the active site and at three surface binding sites. The electron density region observed at the active site, filling subsites-3 through-1, was interpreted in terms of the process of enzyme-catalyzed hydrolysis undergone by maltopentaose. Because the expected conformational changes in the "flexible loop" that constitutes the surface edge of the active site were not observed, the movement of the loop may depend on aglycone site being filled. The crystal structure was refined at 2.01 A resolution to an R factor of 17.0% ( R(free) factor of 19.8%). The final model consists of 3910 protein atoms, one calcium ion, two chloride ions, 103 oligosaccharide atoms, 761 atoms of water molecules, and 23 ethylene glycol atoms.
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'''Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides'''
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Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaccharides.,Payan F, Qian M J Protein Chem. 2003 Apr;22(3):275-84. PMID:12962327<ref>PMID:12962327</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 1ua3" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The structural X-ray map of a pig pancreatic alpha-amylase crystal soaked (and flash-frozen) with a maltopentaose substrate showed a pattern of electron density corresponding to the binding of oligosaccharides at the active site and at three surface binding sites. The electron density region observed at the active site, filling subsites-3 through-1, was interpreted in terms of the process of enzyme-catalyzed hydrolysis undergone by maltopentaose. Because the expected conformational changes in the "flexible loop" that constitutes the surface edge of the active site were not observed, the movement of the loop may depend on aglycone site being filled. The crystal structure was refined at 2.01 A resolution to an R factor of 17.0% ( R(free) factor of 19.8%). The final model consists of 3910 protein atoms, one calcium ion, two chloride ions, 103 oligosaccharide atoms, 761 atoms of water molecules, and 23 ethylene glycol atoms.
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*[[Amylase 3D structures|Amylase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1UA3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UA3 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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Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaccharides., Payan F, Qian M, J Protein Chem. 2003 Apr;22(3):275-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12962327 12962327]
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[[Category: Alpha-amylase]]
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[[Category: Single protein]]
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Payan, F.]]
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[[Category: Payan F]]
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[[Category: Qian, M.]]
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[[Category: Qian M]]
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[[Category: beta-alpha-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:07:27 2008''
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Current revision

Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides

PDB ID 1ua3

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