› 1pba

Solution NMR

THE NMR STRUCTURE OF THE ACTIVATION DOMAIN ISOLATED FROM PORCINE PROCARBOXYPEPTIDASE B

Released:
DOI: 10.2210/pdb1pba/pdb
PDB entry 1pba coloured by chain, ensemble of 20 models, front view.
PDB entry 1pba coloured by chain, ensemble of 20 models, side view.
PDB entry 1pba coloured by chain, ensemble of 20 models, top view.
Source organism: Sus scrofa
Primary publication:
The NMR structure of the activation domain isolated from porcine procarboxypeptidase B.
Vendrell J, Billeter M, Wider G, Avilés FX, Wüthrich K
EMBO J 10 11-5 (1991)
PMID: 1989879

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140836 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxypeptidase B Chain: A
Molecule details ›
Chain: A
Length: 81 amino acids
Theoretical weight: 9.52 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P09955 (Residues: 16-96; Coverage: 20%)
Gene names: CPB, CPB1
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
Expression system: Not provided

Quick links

Citations

2 review citations

Natural protein proteinase inhibitors and their interaction with proteinases.
Bode et al. (1992)
1 more

11 mentions without citation

Chemical shift prediction for protein structure calculation and quality assessment using an optimally parameterized force field.
Nielsen et al. (2012)
10 more