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2vzp

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==ATOMIC RESOLUTION STRUCTURE OF THE C-TERMINAL CBM35 FROM AMYCOLATOPSIS ORIENTALIS EXO-CHITOSANASE CSXA==
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<StructureSection load='2vzp' size='340' side='right' caption='[[2vzp]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
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==Atomic Resolution Structure of the C-terminal CBM35 from Amycolatopsis orientalis exo-chitosanase CsxA==
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<StructureSection load='2vzp' size='340' side='right'caption='[[2vzp]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2vzp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Amycolatopsis_orientalis Amycolatopsis orientalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VZP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VZP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2vzp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis_orientalis Amycolatopsis orientalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VZP FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene><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]] 1.05&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vzt|2vzt]], [[2vzu|2vzu]], [[2vzq|2vzq]], [[2vzo|2vzo]], [[2vzs|2vzs]], [[2vzr|2vzr]], [[2vzv|2vzv]]</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vzp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vzp RCSB], [http://www.ebi.ac.uk/pdbsum/2vzp PDBsum]</span></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=2vzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vzp OCA], [https://pdbe.org/2vzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vzp RCSB], [https://www.ebi.ac.uk/pdbsum/2vzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vzp ProSAT]</span></td></tr>
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<table>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/EBDG_AMYOR EBDG_AMYOR] Hydrolyzes chitosan and chitooligosaccharides with retention of anomeric configuration. Has maximum activity on chitotetraose, chitopentaose and their corresponding alcohols, with a slight decrease in the rate of hydrolysis on longer chains. Has no activity against beta-D-glucopyranoside, beta-D-xylopyranoside, beta-D-mannoside, beta-D-glucuronide, beta-D-galactoside, beta-D-N-acetylgalactosamide, beta-D-N-acetylglucosaminide and alpha-D-N-acetylglucosaminide.<ref>PMID:16316314</ref> <ref>PMID:2351651</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vz/2vzp_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vz/2vzp_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=2vzp ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2vzp" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Amycolatopsis orientalis]]
[[Category: Amycolatopsis orientalis]]
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[[Category: Boraston, A B.]]
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[[Category: Large Structures]]
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[[Category: Bueren, A Lammerts Van.]]
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[[Category: Boraston AB]]
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[[Category: Cbm]]
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[[Category: Lammerts van Bueren A]]
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[[Category: Csxa]]
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[[Category: Family 35]]
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[[Category: Glucuronic acid]]
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[[Category: Hydrolase]]
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Current revision

Atomic Resolution Structure of the C-terminal CBM35 from Amycolatopsis orientalis exo-chitosanase CsxA

PDB ID 2vzp

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