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PDBsum entry 5dhe

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Hydrolase PDB id
5dhe
Contents
Protein chains
100 a.a.
Ligands
GOL ×5
Waters ×194

References listed in PDB file
Key reference
Title Crystal structures of chitin binding domains of chitinase from thermococcus kodakarensis kod1.
Authors Y.Hanazono, K.Takeda, S.Niwa, M.Hibi, N.Takahashi, T.Kanai, H.Atomi, K.Miki.
Ref. Febs Lett, 2016, 590, 298-304. [DOI no: 10.1002/1873-3468.12055]
PubMed id 26823175
Abstract
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-π interactions and the amide group by a hydrogen bond, respectively.
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