3blk

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<StructureSection load='3blk' size='340' side='right'caption='[[3blk]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3blk' size='340' side='right'caption='[[3blk]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3blk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BLK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BLK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3blk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BLK FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGL:4,6-DIDEOXY-4-AMINO-ALPHA-D-GLUCOSE'>AGL</scene>, <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=HMC:5-HYDROXYMETHYL-CHONDURITOL'>HMC</scene></td></tr>
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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&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=AGL:4,6-DIDEOXY-4-AMINO-ALPHA-D-GLUCOSE'>AGL</scene>, <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=HMC:5-HYDROXYMETHYL-CHONDURITOL'>HMC</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1smd|1smd]], [[1mfv|1mfv]], [[1mfu|1mfu]], [[3blp|3blp]]</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=3blk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3blk OCA], [https://pdbe.org/3blk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3blk RCSB], [https://www.ebi.ac.uk/pdbsum/3blk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3blk ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AMY1A, AMY1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3blk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3blk OCA], [http://pdbe.org/3blk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3blk RCSB], [http://www.ebi.ac.uk/pdbsum/3blk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3blk ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMY1A_HUMAN AMY1A_HUMAN] Calcium-binding enzyme that initiates starch digestion in the oral cavity (PubMed:12527308). Catalyzes the hydrolysis of internal (1->4)-alpha-D-glucosidic bonds, yielding a mixture of maltose, isomaltose, small amounts of glucose as well as small linear and branched oligosaccharides called dextrins (PubMed:12527308).<ref>PMID:12527308</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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<jmolCheckbox>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bl/3blk_consurf.spt"</scriptWhenChecked>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bl/3blk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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==See Also==
==See Also==
*[[Amylase 3D structures|Amylase 3D structures]]
*[[Amylase 3D structures|Amylase 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Alpha-amylase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ramasubbu, N]]
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[[Category: Ramasubbu N]]
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[[Category: Calcium]]
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[[Category: Carbohydrate metabolism]]
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[[Category: Chloride]]
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[[Category: Glycoprotein]]
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[[Category: Glycosidase]]
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[[Category: Greek key barrel]]
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[[Category: Hydrolase]]
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[[Category: Metal-binding]]
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[[Category: Pyrrolidone carboxylic acid]]
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[[Category: Secreted]]
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[[Category: Tim barrel]]
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Current revision

Role of aromatic residues in starch binding

PDB ID 3blk

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