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1jfh

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(New page: 200px<br /><applet load="1jfh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jfh, resolution 2.03&Aring;" /> '''STRUCTURE OF A PANCR...)
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[[Image:1jfh.gif|left|200px]]<br /><applet load="1jfh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1jfh, resolution 2.03&Aring;" />
 
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'''STRUCTURE OF A PANCREATIC ALPHA-AMYLASE BOUND TO A SUBSTRATE ANALOGUE AT 2.03 ANGSTROM RESOLUTION'''<br />
 
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==Overview==
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==STRUCTURE OF A PANCREATIC ALPHA-AMYLASE BOUND TO A SUBSTRATE ANALOGUE AT 2.03 ANGSTROM RESOLUTION==
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The structure of pig pancreatic alpha-amylase in complex with carbohydrate, inhibitor and proteinaceous inhibitors is known but the successive events, occurring at the catalytic center still remain to be elucidated. The X-ray, structure analysis of a crystal of pig pancreatic alpha-amylase (PPA, EC, 3.2.1.1.) soaked with an enzyme-resistant substrate analogue, methyl, 4,4'-dithio-alpha-maltotrioside, showed electron density corresponding to, the binding of substrate analogue molecules at the active site and at the, "second binding site." The electron density observed at the active site, was interpreted in terms of overlapping networks of oligosaccharides, which show binding of substrate analogue molecules at subsites prior to, and subsequent to the cleavage site. A weaker patch of density observed at, subsite -1 (using a nomenclature where the site of hydrolysis is taken to, be between subsites -1 and +1) was modeled with water molecules., Conformational changes take place upon substrate analogue binding and the, "flexible loop" that constitutes the surface edge of the active site is, observed in a specific conformation. This confirms that this loop plays an, important role in the recognition and binding of the ligand. The crystal, structure was refined at 2.03 A resolution, to an R-factor of 16.0 (Rfree, 18.5).
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<StructureSection load='1jfh' size='340' side='right'caption='[[1jfh]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1jfh]] 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=1JFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JFH 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]] 2.03&#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>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MA1:1,4-DITHIO-ALPHA-D-GLUCOPYRANOSE'>MA1</scene>, <scene name='pdbligand=MA2:4-S-METHYL-4-THIO-ALPHA-D-GLUCOPYRANOSE'>MA2</scene>, <scene name='pdbligand=MA3:O1-METHYL-4-DEOXY-4-THIO-ALPHA-D-GLUCOSE'>MA3</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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=1jfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jfh OCA], [https://pdbe.org/1jfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jfh RCSB], [https://www.ebi.ac.uk/pdbsum/1jfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jfh ProSAT]</span></td></tr>
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</table>
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== Function ==
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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/jf/1jfh_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=1jfh 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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1JFH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with MA2, MA3, MAN, MA1, CL, HG and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JFH OCA].
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*[[Amylase 3D structures|Amylase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03 A resolution., Qian M, Spinelli S, Driguez H, Payan F, Protein Sci. 1997 Nov;6(11):2285-96. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9385631 9385631]
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[[Category: Large Structures]]
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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: CA]]
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[[Category: CL]]
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[[Category: HG]]
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[[Category: MA1]]
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[[Category: MA2]]
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[[Category: MA3]]
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[[Category: MAN]]
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[[Category: 4'-dithio-alpha-maltotrioside]]
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[[Category: alpha-amylase]]
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[[Category: hydrolase]]
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[[Category: methyl 4]]
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[[Category: o-glycosyl]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:11:50 2007''
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Current revision

STRUCTURE OF A PANCREATIC ALPHA-AMYLASE BOUND TO A SUBSTRATE ANALOGUE AT 2.03 ANGSTROM RESOLUTION

PDB ID 1jfh

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