› 1ll6

X-ray diffraction
2.8Å resolution

STRUCTURE OF THE D169N MUTANT OF C. IMMITIS CHITINASE 1

Released:
DOI: 10.2210/pdb1ll6/pdb
Model geometry
Fit model/data
PDB entry 1ll6 coloured by chain, front view.
PDB entry 1ll6 coloured by chain, side view.
PDB entry 1ll6 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)
Assembly name:
PDBe Complex ID:
PDB-CPX-143199 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU RU200
Spacegroup: P1
Unit cell:
a: 60.89Å b: 78.18Å c: 88.43Å
α: 80.51° β: 82.13° γ: 66.99°
R-values:
R R work R free
0.182 0.182 0.256
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

Design, synthesis, and biological evaluation of an allosteric inhibitor of HSET that targets cancer cells with supernumerary centrosomes.
Watts et al. (2013)