› 1w9p

X-ray diffraction
1.7Å resolution

Specificity and affinity of natural product cyclopentapeptide inhibitors against Aspergillus fumigatus, human and bacterial chitinaseFra

Released:
DOI: 10.2210/pdb1w9p/pdb
PDB entry 1w9p coloured by chain, front view.
PDB entry 1w9p coloured by chain, side view.
PDB entry 1w9p coloured by chain, top view.
Source organism: Aspergillus fumigatus
Primary publication:
Specificity and affinity of natural product cyclopentapeptide inhibitors against A. fumigatus, human, and bacterial chitinases.
Rao FV, Houston DR, Boot RG, Aerts JM, Hodkinson M, Adams DJ, Shiomi K, Omura S, van Aalten DM
Chem Biol 12 65-76 (2005)
PMID: 15664516

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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183289 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endochitinase B1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 433 amino acids
Theoretical weight: 47.66 KDa
Source organism: Aspergillus fumigatus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q873X9 (Residues: 1-433; Coverage: 100%)
Gene name: chiB1
Sequence domains: Glycosyl hydrolases family 18
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 7 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P41
Unit cell:
a: 117.407Å b: 117.407Å c: 99.27Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 0.202
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Insect chitinase and chitinase-like proteins.
Arakane et al. (2010)
12 more

11 mentions without citation

Sequence and structural analysis of the chitinase insertion domain reveals two conserved motifs involved in chitin-binding.
Li et al. (2010)
10 more