› 2ybu

X-ray diffraction
2.25Å resolution

Crystal structure of human acidic chitinase in complex with bisdionin F

Released:
DOI: 10.2210/pdb2ybu/pdb
PDB entry 2ybu coloured by chain, front view.
PDB entry 2ybu coloured by chain, side view.
PDB entry 2ybu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Analyzing airway inflammation with chemical biology: dissection of acidic mammalian chitinase function with a selective drug-like inhibitor.
Sutherland TE, Andersen OA, Betou M, Eggleston IM, Maizels RM, van Aalten D, Allen JE
Chem Biol 18 569-79 (2011)
PMID: 21609838

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, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 381 amino acids
Theoretical weight: 42.63 KDa
Source organism: Homo sapiens
Expression system: Komagataella phaffii GS115
UniProt:
  • Canonical: Q9BZP6 (Residues: 21-398; Coverage: 83%)
Gene name: CHIA
Sequence domains: Glycosyl hydrolases family 18
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GOL 6 x GOL
Ligand CX9 12 x CX9
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 144.781Å b: 149.194Å c: 151.278Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.173 0.219
Expression system: Komagataella phaffii GS115

Quick links

Citations

6 review citations

Macrophage proliferation, provenance, and plasticity in macroparasite infection.
Rückerl et al. (2014)
5 more

2 mentions without citation

PgaB orthologues contain a glycoside hydrolase domain that cleaves deacetylated poly-β(1,6)-N-acetylglucosamine and can disrupt bacterial biofilms.
Little et al. (2018)
1 more