PDBsum entry 5dhe

Hydrolase

PDB id

5dhe

Loading ...

Contents

			Protein chains

					100 a.a.

			Ligands

					GOL ×5

			Waters ×194

PDB id:

5dhe

Links

Name:

Hydrolase

Title:

Crystal structure of chbd3 from thermococcus kodakarensis kod1

Structure:

Chitinase. Chain: a, b. Fragment: chbd3 domain, unp residues 764-863. Synonym: chitinase,containing dual catalytic domains. Engineered: yes

Source:

Thermococcus kodakarensis kod1. Organism_taxid: 69014. Strain: kod1. Gene: pk-chia, tk1765. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.60Å

R-factor:

0.194

R-free:

0.209

Authors:

S.Niwa,M.Hibi,K.Takeda,K.Miki

Key ref:

Y.Hanazono et al. (2016). Crystal structures of chitin binding domains of chitinase from Thermococcus kodakarensis KOD1. Febs Lett, 590, 298-304. PubMed id: 26823175 DOI: 10.1002/1873-3468.12055

Date:

30-Aug-15

Release date:

10-Feb-16

PROCHECK

	Headers

	References

Protein chains

Q9UWR7 (Q9UWR7_THEKO) - Chitinase from Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

Seq: Struc:

Seq: Struc:

Seq: Struc:					1215 a.a. 100 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.3.2.1.14 - chitinase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

Hydrolysis of the 1,4-beta-linkages of N-acetyl-D-glucosamine polymers of chitin.

DOI no: 10.1002/1873-3468.12055	Febs Lett 590:298-304 (2016)
PubMed id: 26823175

Crystal structures of chitin binding domains of chitinase from Thermococcus kodakarensis KOD1.
Y.Hanazono, K.Takeda, S.Niwa, M.Hibi, N.Takahashi, T.Kanai, H.Atomi, K.Miki.

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.