› 2aih

Solution NMR

1H-NMR solution structure of a trypsin/chymotrypsin Bowman-Birk inhibitor from Lens culinaris.

Released:
DOI: 10.2210/pdb2aih/pdb
PDB entry 2aih coloured by chain, ensemble of 20 models, front view.
PDB entry 2aih coloured by chain, ensemble of 20 models, side view.
PDB entry 2aih coloured by chain, ensemble of 20 models, top view.
Source organism: Lens culinaris
Primary publication:
Inhibitory properties and solution structure of a potent Bowman-Birk protease inhibitor from lentil (Lens culinaris, L) seeds.
Ragg EM, Galbusera V, Scarafoni A, Negri A, Tedeschi G, Consonni A, Sessa F, Duranti M
FEBS J 273 4024-39 (2006)
PMID: 16889634

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186666 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bowman-Birk type proteinase inhibitor Chain: A
Molecule details ›
Chain: A
Length: 67 amino acids
Theoretical weight: 7.47 KDa
Source organism: Lens culinaris
UniProt:
  • Canonical: Q8W4Y8 (Residues: 43-109; Coverage: 82%)
Sequence domains: Bowman-Birk serine protease inhibitor family
Structure domains: Cysteine Protease (Bromelain) Inhibitor, subunit H

Ligands and Environments

1 bound ligand:
Ligand CL 11 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing molecular dynamics matrix relaxation energy minimization

Quick links

Citations

3 review citations

Bowman-Birk inhibitors from legumes as colorectal chemopreventive agents.
Clemente et al. (2014)
2 more

2 mentions without citation

Plant Protease Inhibitors in Therapeutics-Focus on Cancer Therapy.
Srikanth et al. (2016)
1 more