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1wzl
From Proteopedia
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<StructureSection load='1wzl' size='340' side='right'caption='[[1wzl]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1wzl' size='340' side='right'caption='[[1wzl]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1wzl]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1wzl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WZL FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wzl OCA], [https://pdbe.org/1wzl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wzl RCSB], [https://www.ebi.ac.uk/pdbsum/1wzl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wzl ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/NEPU2_THEVU NEPU2_THEVU] Hydrolyzes pullulan efficiently but only a small amount of starch. Endohydrolysis of 1,4-alpha-glucosidic linkages in pullulan to form panose. Cleaves also (1-6)-alpha-glucosidic linkages to form maltotriose. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 43649]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Thermoactinomyces vulgaris]] |
| - | [[Category: Ichikawa | + | [[Category: Ichikawa K]] |
| - | [[Category: Kamitori | + | [[Category: Kamitori S]] |
| - | [[Category: Mizuno | + | [[Category: Mizuno M]] |
| - | [[Category: Nishikawa | + | [[Category: Nishikawa A]] |
| - | [[Category: Ohtaki | + | [[Category: Ohtaki A]] |
| - | [[Category: Sakano | + | [[Category: Sakano Y]] |
| - | [[Category: Shimura | + | [[Category: Shimura Y]] |
| - | [[Category: Tonozuka | + | [[Category: Tonozuka T]] |
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Current revision
Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) mutatnt R469L
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