1ffq: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ffq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FFQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FFQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ffq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FFQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FFQ FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMI:ALLOSAMIZOLINE'>AMI</scene>, <scene name='pdbligand=NAA:N-ACETYL-D-ALLOSAMINE'>NAA</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMI:ALLOSAMIZOLINE'>AMI</scene>, <scene name='pdbligand=NAA:N-ACETYL-D-ALLOSAMINE'>NAA</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1edq|1edq]], [[1ehn|1ehn]], [[1eib|1eib]], [[1ffr|1ffr]], [[1ctn|1ctn]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1edq|1edq]], [[1ehn|1ehn]], [[1eib|1eib]], [[1ffr|1ffr]], [[1ctn|1ctn]]</td></tr> | ||
<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ffq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ffq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ffq RCSB], [http://www.ebi.ac.uk/pdbsum/1ffq 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=1ffq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ffq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ffq RCSB], [http://www.ebi.ac.uk/pdbsum/1ffq PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Chitinase]] | [[Category: Chitinase]] | ||
[[Category: Serratia marcescens]] | [[Category: Serratia marcescens]] | ||
[[Category: Papanikolau, Y | [[Category: Papanikolau, Y]] | ||
[[Category: Petratos, K | [[Category: Petratos, K]] | ||
[[Category: Tavlas, G | [[Category: Tavlas, G]] | ||
[[Category: Vorgias, C E | [[Category: Vorgias, C E]] | ||
[[Category: Enzyme-inhibitor complex]] | [[Category: Enzyme-inhibitor complex]] | ||
[[Category: Glycosyl hydrolase]] | [[Category: Glycosyl hydrolase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 02:05, 23 December 2014
CRYSTAL STRUCTURE OF CHITINASE A COMPLEXED WITH ALLOSAMIDINCRYSTAL STRUCTURE OF CHITINASE A COMPLEXED WITH ALLOSAMIDIN
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe purification scheme of chitinase A (ChiA) from S. marcescens has been extensively revised. The pure enzyme crystallizes readily under new crystallization conditions. The ChiA crystal structure has been refined to 1.55 A resolution and the crystal structure of ChiA co-crystallized with the inhibitor allosamidin has been refined to 1.9 A resolution. Allosamidin is located in the deep active-site tunnel of ChiA and interacts with three important residues: Glu315, the proton donor of the catalysis, Asp313, which adopts two conformations in the native structure but is oriented towards Glu315 in the inhibitor complex, and Tyr390, which lies opposite Glu315 in the active-site tunnel. De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin.,Papanikolau Y, Tavlas G, Vorgias CE, Petratos K Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):400-3. Epub 2003, Jan 23. PMID:12554965[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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