› 3rm8

X-ray diffraction
1.8Å 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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189864 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acidic mammalian chitinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 395 amino acids
Theoretical weight: 44.2 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: Q9BZP6 (Residues: 22-408; Coverage: 85%)
Gene name: CHIA
Sequence domains: Glycosyl hydrolases family 18
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand RM8 2 x RM8
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P212121
Unit cell:
a: 63.684Å b: 89.248Å c: 125.804Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.199 0.224
Expression system: Cricetulus griseus

Quick links

Citations

4 review citations

Developing inhibitors of glycan processing enzymes as tools for enabling glycobiology.
Gloster et al. (2012)
3 more

1 mention without citation

Structural characterization of ligand binding and pH-specific enzymatic activity of mouse Acidic Mammalian Chitinase.
Díaz et al. (2023)