1byb: Difference between revisions

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[[Image:1byb.png|left|200px]]


{{STRUCTURE_1byb|  PDB=1byb  |  SCENE=  }}
==CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS==
 
<StructureSection load='1byb' size='340' side='right'caption='[[1byb]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
===CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1byb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BYB FirstGlance]. <br>
{{ABSTRACT_PUBMED_8011643}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1byb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1byb OCA], [https://pdbe.org/1byb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1byb RCSB], [https://www.ebi.ac.uk/pdbsum/1byb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1byb ProSAT]</span></td></tr>
[[1byb]] is a 1 chain structure of [[Alpha-Amylase]] with sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYB OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMYB_SOYBN AMYB_SOYBN]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/by/1byb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1byb ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Alpha-Amylase|Alpha-Amylase]]
*[[Amylase 3D structures|Amylase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:008011643</ref><ref group="xtra">PMID:015794648</ref><references group="xtra"/>
[[Category: Beta-amylase]]
[[Category: Glycine max]]
[[Category: Glycine max]]
[[Category: Degano, M.]]
[[Category: Large Structures]]
[[Category: Hehre, E J.]]
[[Category: Degano M]]
[[Category: Mikami, B.]]
[[Category: Hehre EJ]]
[[Category: Sacchettini, J C.]]
[[Category: Mikami B]]
[[Category: Sacchettini JC]]

Latest revision as of 09:39, 7 February 2024

CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSISCRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS

Structural highlights

1byb is a 1 chain structure with sequence from Glycine max. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AMYB_SOYBN

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1byb, resolution 1.90Å

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