1gbg

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<StructureSection load='1gbg' size='340' side='right'caption='[[1gbg]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1gbg' size='340' side='right'caption='[[1gbg]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1gbg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"clostridium_licheniforme"_weigmann_1898 "clostridium licheniforme" weigmann 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GBG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1gbg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GBG FirstGlance]. <br>
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</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></td></tr>
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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]] 1.8&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73] </span></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></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=1gbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbg OCA], [https://pdbe.org/1gbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gbg RCSB], [https://www.ebi.ac.uk/pdbsum/1gbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gbg ProSAT]</span></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=1gbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbg OCA], [https://pdbe.org/1gbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gbg RCSB], [https://www.ebi.ac.uk/pdbsum/1gbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gbg ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GUB_BACLI GUB_BACLI]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1gbg ConSurf].
</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=1gbg ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The crystal structure of the 1,3-1,4-beta-D-glucan 4-glucanohydrolase from Bacillus licheniformis is solved at a resolution of 1.8 A and refined to R = 16.5%. The protein has a similar beta-sandwich structure as the homologous enzyme from Bacillus macerans and the hybrid H(A16-M). This demonstrates that the jellyroll fold of these proteins is remarkably rigid and only weakly influenced by crystal contacts. The crystal structure permits to extend mechanistic considerations derived for the B. licheniformis enzyme to the entire class of bacterial 1,3-1,4-beta-D-glucan 4-glucanohydrolases.
 
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Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8 A resolution.,Hahn M, Pons J, Planas A, Querol E, Heinemann U FEBS Lett. 1995 Oct 30;374(2):221-4. PMID:7589539<ref>PMID:7589539</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1gbg" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
*[[Glucanase 3D structures|Glucanase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Clostridium licheniforme weigmann 1898]]
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[[Category: Bacillus licheniformis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Licheninase]]
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[[Category: Hahn M]]
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[[Category: Hahn, M]]
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[[Category: Heinemann U]]
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[[Category: Heinemann, U]]
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Revision as of 11:20, 27 March 2024

BACILLUS LICHENIFORMIS BETA-GLUCANASE

PDB ID 1gbg

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