View source for 5dhd


==Crystal structure of ChBD2 from Thermococcus kodakarensis KOD1==
<StructureSection load='5dhd' size='340' side='right'caption='[[5dhd]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5dhd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DHD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.27&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PE3:3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL'>PE3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5dhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dhd OCA], [https://pdbe.org/5dhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dhd RCSB], [https://www.ebi.ac.uk/pdbsum/5dhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dhd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9UWR7_THEKO Q9UWR7_THEKO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Chitinase from T. kodakarensis (TkChiA) catalyzes the hydrolysis of chitin. The enzyme consists of two catalytic and three binding domains (ChBD1, ChBD2 and ChBD3). ChBD2 and ChBD3 can bind to not only chitin but also cellulose. In both domains, the intervals of the side chains of the three tryptophan residues, which are located on the molecular surface, correspond to twice the length of the lattice of the chitin. A binding model with crystalline chitin implies that the tryptophan residues and a glutamate residue interact with the hexose ring by CH-pi interactions and the amide group by a hydrogen bond, respectively.

Crystal structures of chitin binding domains of chitinase from Thermococcus kodakarensis KOD1.,Hanazono Y, Takeda K, Niwa S, Hibi M, Takahashi N, Kanai T, Atomi H, Miki K FEBS Lett. 2016 Jan;590(2):298-304. doi: 10.1002/1873-3468.12055. Epub 2016 Jan, 20. PMID:26823175<ref>PMID:26823175</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5dhd" style="background-color:#fffaf0;"></div>

==See Also==
*[[Chitinase 3D structures|Chitinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermococcus kodakarensis KOD1]]
[[Category: Hibi M]]
[[Category: Miki K]]
[[Category: Niwa S]]
[[Category: Takeda K]]