› 1guv

X-ray diffraction
2.35Å resolution

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-171609 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chitotriosidase-1 Chain: A
Molecule details ›
Chain: A
Length: 366 amino acids
Theoretical weight: 40.9 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q13231 (Residues: 22-387; Coverage: 82%)
Gene name: CHIT1
Sequence domains: Glycosyl hydrolases family 18
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand EDO 10 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P43212
Unit cell:
a: 93.258Å b: 93.258Å c: 89.797Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.262

Quick links

Citations

18 review citations

Exploring the full spectrum of macrophage activation.
Mosser et al. (2008)
17 more

9 mentions without citation

Triad of polar residues implicated in pH specificity of acidic mammalian chitinase.
Olland et al. (2009)
8 more