X-ray diffraction
2Å resolution

Crystal Structure of the Ostrinia furnacalis Group I Chitinase catalytic domain E148Q mutant

Source organism: Ostrinia furnacalis
Entry authors: Chen L, Liu T, Zhou Y, Chen Q, Shen X, Yang Q

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Chitinase Chain: A
Molecule details ›
Chain: A
Length: 395 amino acids
Theoretical weight: 44.99 KDa
Source organism: Ostrinia furnacalis
Expression system: Komagataella pastoris
  • Canonical: Q2V6H4 (Residues: 19-407; Coverage: 73%)
Sequence domains: Glycosyl hydrolases family 18
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P65
Unit cell:
a: 94.241Å b: 94.241Å c: 122.195Å
α: 90° β: 90° γ: 120°
R R work R free
0.16 0.158 0.186
Expression system: Komagataella pastoris