3voc
From Proteopedia
(Difference between revisions)
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==Crystal structure of the catalytic domain of beta-amylase from paenibacillus polymyxa== | ==Crystal structure of the catalytic domain of beta-amylase from paenibacillus polymyxa== | ||
| - | <StructureSection load='3voc' size='340' side='right' caption='[[3voc]], [[Resolution|resolution]] 1.95Å' scene=''> | + | <StructureSection load='3voc' size='340' side='right'caption='[[3voc]], [[Resolution|resolution]] 1.95Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3voc]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3voc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"aerobacillus_polymyxa"_(prazmowski_1880)_donker_1926 "aerobacillus polymyxa" (prazmowski 1880) donker 1926]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VOC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VOC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | + | </td></tr><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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-amylase Beta-amylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.2 3.2.1.2] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3voc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3voc OCA], [https://pdbe.org/3voc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3voc RCSB], [https://www.ebi.ac.uk/pdbsum/3voc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3voc ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/AMYB_PAEPO AMYB_PAEPO]] The precursor protein is proteolytically cleaved to produce multiform beta-amylases and a 48 kDa alpha-amylase after secretion. |
==See Also== | ==See Also== | ||
| - | *[[Amylase|Amylase]] | + | *[[Amylase 3D structures|Amylase 3D structures]] |
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Beta-amylase]] | [[Category: Beta-amylase]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Fujioka, T]] | [[Category: Fujioka, T]] | ||
[[Category: Nakaniwa, T]] | [[Category: Nakaniwa, T]] | ||
Revision as of 18:55, 27 July 2022
Crystal structure of the catalytic domain of beta-amylase from paenibacillus polymyxa
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