› 3n1a

X-ray diffraction
2Å resolution

Crystal stricture of E145G/Y227F chitinase in complex with cyclo-(L-His-L-Pro) from Bacillus cereus NCTU2

Released:
DOI: 10.2210/pdb3n1a/pdb
PDB entry 3n1a coloured by chain, front view.
PDB entry 3n1a coloured by chain, side view.
PDB entry 3n1a coloured by chain, top view.
Source organism: Bacillus cereus
Primary publication:
Crystal structures of Bacillus cereus NCTU2 chitinase complexes with chitooligomers reveal novel substrate binding for catalysis: a chitinase without chitin binding and insertion domains.
Hsieh YC, Wu YJ, Chiang TY, Kuo CY, Shrestha KL, Chao CF, Huang YC, Chuankhayan P, Wu WG, Li YK, Chen CJ
J Biol Chem 285 31603-15 (2010)
PMID: 20685646

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112057 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
chitinase Chain: A
Molecule details ›
Chain: A
Length: 333 amino acids
Theoretical weight: 36.18 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli
UniProt:
  • Canonical: D0VV09 (Residues: 28-360; Coverage: 100%)
Sequence domains: Glycosyl hydrolases family 18
Structure domains: Glycosidases

Ligands and Environments

1 bound ligand:
Ligand CHQ 1 x CHQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P212121
Unit cell:
a: 48.737Å b: 75.045Å c: 79.081Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.199 0.238
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The chitinolytic machinery of Serratia marcescens--a model system for enzymatic degradation of recalcitrant polysaccharides.
Vaaje-Kolstad et al. (2013)
2 more

3 mentions without citation

The solvent component of macromolecular crystals.
Weichenberger et al. (2015)
2 more