5DHE

Crystal structure of ChBD3 from Thermococcus kodakarensis KOD1

Summary for 5DHE

• Entry DOI: 10.2210/pdb5dhe/pdb
• Related: 5DHD
• Descriptor: Chitinase, GLYCEROL (3 entities in total)
• Functional Keywords: chitin, chitinase, chitin binding domain, hydrolase
• Biological source: Thermococcus kodakarensis KOD1
• Total number of polymer chains: 2
• Total formula weight: 22476.86

Authors

Niwa, S.,Hibi, M.,Takeda, K.,Miki, K. (deposition date: 2015-08-30, release date: 2016-02-10, Last modification date: 2024-03-20)

Primary citation

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., 590:298-304, 2016

PubMed 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.

PubMed: 26823175
DOI: 10.1002/1873-3468.12055

Experimental method

X-RAY DIFFRACTION (1.6 Å)