3qt4

X-ray diffraction
2.11Å resolution

Structure of digestive procathepsin L 3 of Tenebrio molitor larval midgut

Released:

Function and Biology Details

Reaction catalysed:
Similar to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-182224 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin-L-like midgut cysteine proteinase Chain: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 36.48 KDa
Source organism: Tenebrio molitor
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7YXL2 (Residues: 19-330; Coverage: 100%)
Sequence domains:
Structure domains: Cysteine proteinases

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: C2
Unit cell:
a: 57.634Å b: 89.322Å c: 70.076Å
α: 90° β: 92.5° γ: 90°
R-values:
R R work R free
0.16 0.158 0.201
Expression system: Escherichia coli