2c1c

X-ray diffraction
2.3Å resolution

Structural basis of the resistance of an insect carboxypeptidase to plant protease inhibitors

Released:

Function and Biology Details

Reaction catalysed:
Preferential release of a C-terminal lysine or arginine amino acid.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174805 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxypeptidase B Chains: A, B
Molecule details ›
Chains: A, B
Length: 312 amino acids
Theoretical weight: 35.12 KDa
Source organism: Helicoverpa zea
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q3T905 (Residues: 117-428; Coverage: 75%)
Gene name: CPB
Sequence domains: Zinc carboxypeptidase
Structure domains: Zn peptidases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P21
Unit cell:
a: 42.012Å b: 58.339Å c: 146.564Å
α: 90° β: 89.87° γ: 90°
R-values:
R R work R free
0.215 0.215 0.292
Expression system: Komagataella pastoris