4mst

X-ray diffraction
1.93Å resolution

Crystal Structure of a putative catalytic domain of a chitinase-like protein (HbCLP1) from Hevea brasiliensis

Released:

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:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-188203 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inactive chitinase-like protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 242 amino acids
Theoretical weight: 26.55 KDa
Source organism: Hevea brasiliensis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q949H3 (Residues: 73-314; Coverage: 82%)
Gene names: CHI-L1, RQ30
Sequence domains: Chitinase class I
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Unit cell:
a: 111.106Å b: 40.415Å c: 111.854Å
α: 90° β: 96.73° γ: 90°
R-values:
R R work R free
0.168 0.166 0.202
Expression system: Escherichia coli BL21(DE3)