› 1itx

X-ray diffraction
1.1Å resolution

Catalytic Domain of Chitinase A1 from Bacillus circulans WL-12

Released:
DOI: 10.2210/pdb1itx/pdb
PDB entry 1itx coloured by chain, front view.
PDB entry 1itx coloured by chain, side view.
PDB entry 1itx coloured by chain, top view.
Source organism: Niallia circulans
Primary publication:
Three-dimensional structure of the catalytic domain of chitinase A1 from Bacillus circulans WL-12 at a very high resolution
Matsumoto T, Nonaka T, Hashimoto M, Watanabe T, Mitsui Y
Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci. 75 269-274 (1999)

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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148998 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chitinase A1 Chain: A
Molecule details ›
Chain: A
Length: 419 amino acids
Theoretical weight: 45.53 KDa
Source organism: Niallia circulans
Expression system: Escherichia coli
UniProt:
  • Canonical: P20533 (Residues: 33-451; Coverage: 62%)
Gene name: chiA1
Sequence domains: Glycosyl hydrolases family 18
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand GOL 11 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P1
Unit cell:
a: 43.007Å b: 46.839Å c: 55.7Å
α: 109.293° β: 95.455° γ: 116.68°
R-values:
R R work R free
0.117 0.116 0.137
Expression system: Escherichia coli

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Citations

20 mentions without citation

Sequence and structural analysis of the chitinase insertion domain reveals two conserved motifs involved in chitin-binding.
Li et al. (2010)
19 more