› 1ll4

X-ray diffraction
2.8Å resolution

STRUCTURE OF C. IMMITIS CHITINASE 1 COMPLEXED WITH ALLOSAMIDIN

Released:
DOI: 10.2210/pdb1ll4/pdb
PDB entry 1ll4 coloured by chain, front view.
PDB entry 1ll4 coloured by chain, side view.
PDB entry 1ll4 coloured by chain, top view.
Source organism: Coccidioides immitis
Primary publication:
The structure of an allosamidin complex with the Coccidioides immitis chitinase defines a role for a second acid residue in substrate-assisted mechanism.
Bortone K, Monzingo AF, Ernst S, Robertus JD
J Mol Biol 320 293-302 (2002)
PMID: 12079386

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:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Endochitinase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 392 amino acids
Theoretical weight: 43.71 KDa
Source organism: Coccidioides immitis
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CB51 (Residues: 36-427; Coverage: 96%)
Gene names: CPSG_08657, CTS1
Sequence domains: Glycosyl hydrolases family 18
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAA
Carbohydrate polymer
1 bound ligand:
Ligand AMI 4 x AMI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P1
Unit cell:
a: 61.045Å b: 78.19Å c: 88.457Å
α: 80.61° β: 82.27° γ: 66.72°
R-values:
R R work R free
0.197 0.197 0.258
Expression system: Escherichia coli

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Citations

7 review citations

Fungal chitinases: diversity, mechanistic properties and biotechnological potential.
Hartl et al. (2012)
6 more

1 mention without citation

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