1o6x

Solution NMR

NMR solution structure of the activation domain of human procarboxypeptidase A2

Released:

Function and Biology Details

Reaction catalysed:
Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155697 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxypeptidase A2 Chain: A
Molecule details ›
Chain: A
Length: 81 amino acids
Theoretical weight: 9.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P48052 (Residues: 16-96; Coverage: 20%)
Gene name: CPA2
Sequence domains: Carboxypeptidase activation peptide
Structure domains: Metallocarboxypeptidase-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 58%
Expression system: Escherichia coli K-12