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<StructureSection load='1ctn' size='340' side='right'caption='[[1ctn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1ctn' size='340' side='right'caption='[[1ctn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ctn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_marcescens"_(bizio_1823)_trevisan_in_de_toni_and_trevisan_1889 "bacillus marcescens" (bizio 1823) trevisan in de toni and trevisan 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CTN FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ctn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CTN FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] </span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=1ctn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ctn OCA], [https://pdbe.org/1ctn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ctn RCSB], [https://www.ebi.ac.uk/pdbsum/1ctn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ctn 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=1ctn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ctn OCA], [https://pdbe.org/1ctn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ctn RCSB], [https://www.ebi.ac.uk/pdbsum/1ctn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ctn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CHIA_SERMA CHIA_SERMA]
== 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=1ctn 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=1ctn ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: Chitinases cleave the beta-1-4-glycosidic bond between the N-acetyl-D-glucosamine units of which chitin is comprised. Chitinases are present in plants, bacteria and fungi, but whereas structures are available for two prototypic plant enzymes, no structure is available for a bacterial or fungal chitinase. RESULTS: To redress this imbalance, the structure of native chitinase A from Serratia marcescens has been solved by multiple isomorphous replacement and refined at 2.3 A resolution, resulting in a crystallographic R-factor of 16.2%. The enzyme comprises three domains: an all beta-strand amino-terminal domain, a catalytic alpha/beta-barrel domain, and a small alpha+beta-fold domain. There are several residues with unusual geometries in the structure. Structure determination of chitinase A in complex with N,N',N",N"'-tetra-acetylo-chitotetraose, together with biochemical and sequence analysis data, enabled the positions of the active-site and catalytic residues to be proposed. CONCLUSIONS: The reaction mechanism seems to be similar to that of lysozyme and most other glycosylhydrolases, i.e. general acid-base catalysis. The role of the amino-terminal domain could not be identified, but it has similarities to the fibronectin III domain. This domain may possibly facilitate the interaction of chitinase A with chitin.
Crystal structure of a bacterial chitinase at 2.3 A resolution.,Perrakis A, Tews I, Dauter Z, Oppenheim AB, Chet I, Wilson KS, Vorgias CE Structure. 1994 Dec 15;2(12):1169-80. PMID:7704527<ref>PMID:7704527</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ctn" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Chitinase|Chitinase]]
*[[Chitinase|Chitinase]]
*[[Chitinase 3D structures|Chitinase 3D structures]]
*[[Chitinase 3D structures|Chitinase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chitinase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Dauter, Z]]
[[Category: Serratia marcescens]]
[[Category: Perrakis, A]]
[[Category: Dauter Z]]
[[Category: Tews, I]]
[[Category: Perrakis A]]
[[Category: Vorgias, C E]]
[[Category: Tews I]]
[[Category: Wilson, K S]]
[[Category: Vorgias CE]]
[[Category: Wilson KS]]
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