› 3hbe

X-ray diffraction
1.55Å resolution

Class IV chitinase structure from Picea abies at 1.55A

Released:
DOI: 10.2210/pdb3hbe/pdb
PDB entry 3hbe coloured by chain, front view.
PDB entry 3hbe coloured by chain, side view.
PDB entry 3hbe coloured by chain, top view.
Source organism: Picea abies
Primary publication:
The first crystal structures of a family 19 class IV chitinase: the enzyme from Norway spruce.
Ubhayasekera W, Rawat R, Ho SW, Wiweger M, Von Arnold S, Chye ML, Mowbray SL
Plant Mol Biol 71 277-89 (2009)
PMID: 19629717

Function and Biology Details

Reaction catalysed: 
Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180504 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chitin-binding type-1 domain-containing protein Chain: X
Molecule details ›
Chain: X
Length: 204 amino acids
Theoretical weight: 21.53 KDa
Source organism: Picea abies
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q6WSR8 (Residues: 73-276; Coverage: 82%)
Sequence domains: Chitinase class I
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MXE 1 x MXE
Ligand ACT 1 x ACT
Ligand FOR 1 x FOR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21212
Unit cell:
a: 67.194Å b: 65.792Å c: 36.496Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.163 0.194
Expression system: Komagataella pastoris

Quick links

Citations

2 review citations

Chitinase: diversity, limitations, and trends in engineering for suitable applications.
Oyeleye et al. (2018)
1 more

3 mentions without citation

Crystal structures of the catalytic domain of a novel glycohydrolase family 23 chitinase from Ralstonia sp. A-471 reveals a unique arrangement of the catalytic residues for inverting chitin hydrolysis.
Arimori et al. (2013)
2 more