› 1h20

Solution NMR

Solution structure of the potato carboxypeptidase inhibitor

Released:
DOI: 10.2210/pdb1h20/pdb
PDB entry 1h20 coloured by chain, ensemble of 25 models, front view.
PDB entry 1h20 coloured by chain, ensemble of 25 models, side view.
PDB entry 1h20 coloured by chain, ensemble of 25 models, top view.
Source organism: Solanum tuberosum
Primary publication:
Structure and dynamics of the potato carboxypeptidase inhibitor by 1H and 15N NMR.
González C, Neira JL, Ventura S, Bronsoms S, Rico M, Avilés FX
Proteins 50 410-22 (2003)
PMID: 12557184

Function and Biology Details

Biochemical function:
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-133930 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallocarboxypeptidase inhibitor Chain: A
Molecule details ›
Chain: A
Length: 39 amino acids
Theoretical weight: 4.31 KDa
Source organism: Solanum tuberosum
Expression system: Escherichia coli
UniProt:
  • Canonical: P01075 (Residues: 1-39; Coverage: 100%)
Sequence domains: Carboxypeptidase A inhibitor

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: RESTRAINED MOLECULAR DYNAMICS
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Complementation of intramolecular interactions for structural-functional stability of plant serine proteinase inhibitors.
Joshi et al. (2013)
2 more

8 mentions without citation

Peptide-based protease inhibitors from plants.
Hellinger et al. (2019)
7 more