2a3c
From Proteopedia
(Difference between revisions)
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<StructureSection load='2a3c' size='340' side='right' caption='[[2a3c]], [[Resolution|resolution]] 2.07Å' scene=''> | <StructureSection load='2a3c' size='340' side='right' caption='[[2a3c]], [[Resolution|resolution]] 2.07Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2a3c]] is a 2 chain structure | + | <table><tr><td colspan='2'>[[2a3c]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A3C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A3C FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PNX:3,7-DIMETHYL-1-(5-OXOHEXYL)-3,7-DIHYDRO-1H-PURINE-2,6-DIONE'>PNX</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PNX:3,7-DIMETHYL-1-(5-OXOHEXYL)-3,7-DIHYDRO-1H-PURINE-2,6-DIONE'>PNX</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w9p|1w9p]], [[1w9v|1w9v]], [[1w9u|1w9u]], [[2a3a|2a3a]], [[2a3b|2a3b]], [[2a3e|2a3e]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w9p|1w9p]], [[1w9v|1w9v]], [[1w9u|1w9u]], [[2a3a|2a3a]], [[2a3b|2a3b]], [[2a3e|2a3e]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] </span></td></tr> | ||
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a3c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2a3c RCSB], [http://www.ebi.ac.uk/pdbsum/2a3c PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a3c OCA], [http://pdbe.org/2a3c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a3c RCSB], [http://www.ebi.ac.uk/pdbsum/2a3c PDBsum]</span></td></tr> |
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/CHIB1_ASPFM CHIB1_ASPFM]] Major secreted chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Plays a role in the morphogenesis and autolysis (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
+ | <div class="pdbe-citations 2a3c" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Aspergillus fumigatus]] | ||
[[Category: Chitinase]] | [[Category: Chitinase]] | ||
[[Category: Aalten, D M.F van]] | [[Category: Aalten, D M.F van]] |
Revision as of 08:57, 11 September 2015
Crystal structure of Aspergillus fumigatus chitinase B1 in complex with pentoxifylline
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