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| | <StructureSection load='5dhe' size='340' side='right'caption='[[5dhe]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='5dhe' size='340' side='right'caption='[[5dhe]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5dhe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_kodakaraensis_(strain_kod1) Pyrococcus kodakaraensis (strain kod1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DHE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5dhe]] is a 2 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=5DHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DHE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dhd|5dhd]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pk-chiA, TK1765 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69014 Pyrococcus kodakaraensis (strain KOD1)])</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=5dhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dhe OCA], [https://pdbe.org/5dhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dhe RCSB], [https://www.ebi.ac.uk/pdbsum/5dhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dhe ProSAT]</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=5dhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dhe OCA], [http://pdbe.org/5dhe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dhe RCSB], [http://www.ebi.ac.uk/pdbsum/5dhe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dhe ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9UWR7_THEKO Q9UWR7_THEKO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chitinase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hibi, M]] | + | [[Category: Thermococcus kodakarensis KOD1]] |
| - | [[Category: Miki, K]] | + | [[Category: Hibi M]] |
| - | [[Category: Niwa, S]] | + | [[Category: Miki K]] |
| - | [[Category: Takeda, K]] | + | [[Category: Niwa S]] |
| - | [[Category: Chitin]]
| + | [[Category: Takeda K]] |
| - | [[Category: Chitin binding domain]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
Q9UWR7_THEKO
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hanazono Y, Takeda K, Niwa S, Hibi M, Takahashi N, Kanai T, Atomi H, Miki K. Crystal structures of chitin binding domains of chitinase from Thermococcus kodakarensis KOD1. FEBS Lett. 2016 Jan;590(2):298-304. doi: 10.1002/1873-3468.12055. Epub 2016 Jan, 20. PMID:26823175 doi:http://dx.doi.org/10.1002/1873-3468.12055
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