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1gai

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(New page: 200px<br /> <applet load="1gai" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gai, resolution 1.7&Aring;" /> '''GLUCOAMYLASE-471 COM...)
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[[Image:1gai.gif|left|200px]]<br />
 
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<applet load="1gai" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gai, resolution 1.7&Aring;" />
 
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'''GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE'''<br />
 
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==Overview==
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==GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE==
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Crystal structures at pH 4 of complexes of glucoamylase from Aspergillus, awamori var. X100 with the pseudotetrasaccharides D-gluco-dihydroacarbose, and acarbose have been refined to R-factors of 0.147 and 0.131 against, data to 1.7- and 2.0-A resolution, respectively. The two inhibitors bind, in nearly identical manners, each exhibiting a dual binding mode with, respect to the location of the last sugar residues. The reduced affinity, of D-gluco-dihydroacarbose (K1 = 10(-8) M) relative to acarbose (K1 =, 10(-12) M) may stem in part from the weakening of hydrogen bonds of the, catalytic water (Wat 500) to the enzyme. Steric contacts between the, nonreducing end of D-gluco-dihydroacarbose and the catalytic water perturb, Wat 500 from its site of optimal hydrogen bonding to the active ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8679589 (full description)]]
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<StructureSection load='1gai' size='340' side='right'caption='[[1gai]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gai]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_awamori Aspergillus awamori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GAI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GAI 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]] 1.7&#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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900061:dihydro-alpha-acarbose'>PRD_900061</scene>, <scene name='pdbligand=RY7:4,6-dideoxy-4-{[(1S,2S,3S,4R,5R)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]amino}-alpha-D-glucopyranose'>RY7</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=1gai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gai OCA], [https://pdbe.org/1gai PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gai RCSB], [https://www.ebi.ac.uk/pdbsum/1gai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gai ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMYG_ASPAW AMYG_ASPAW]
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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/ga/1gai_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=1gai 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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1GAI is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ ]] with MAN and GAC as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.3 3.2.1.3]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GAI OCA]].
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*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
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*[[Amylase 3D structures|Amylase 3D structures]]
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==Reference==
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*[[Cation-pi interactions|Cation-pi interactions]]
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Crystallographic complexes of glucoamylase with maltooligosaccharide analogs: relationship of stereochemical distortions at the nonreducing end to the catalytic mechanism., Aleshin AE, Stoffer B, Firsov LM, Svensson B, Honzatko RB, Biochemistry. 1996 Jun 25;35(25):8319-28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8679589 8679589]
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__TOC__
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[[Category: Single protein]]
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</StructureSection>
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[[Category: Aleshin, A.E.]]
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[[Category: Aspergillus awamori]]
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[[Category: Firsov, L.M.]]
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[[Category: Large Structures]]
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[[Category: Honzatko, R.B.]]
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[[Category: Aleshin AE]]
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[[Category: Stoffer, B.]]
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[[Category: Firsov LM]]
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[[Category: Svensson, B.]]
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[[Category: Honzatko RB]]
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[[Category: GAC]]
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[[Category: Stoffer B]]
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[[Category: MAN]]
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[[Category: Svensson B]]
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[[Category: glycoprotein]]
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[[Category: glycosidase]]
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[[Category: hydrolase]]
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[[Category: polysaccharide degradation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 16:14:42 2007''
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Current revision

GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE

PDB ID 1gai

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