› 1bip

Solution NMR

BIFUNCTIONAL PROTEINASE INHIBITOR TRYPSIN/A-AMYLASE FROM SEEDS OF RAGI (ELEUSINE CORACANA GAERTNERI)

Released:
DOI: 10.2210/pdb1bip/pdb
PDB entry 1bip coloured by chain, ensemble of 20 models, front view.
PDB entry 1bip coloured by chain, ensemble of 20 models, side view.
PDB entry 1bip coloured by chain, ensemble of 20 models, top view.
Source organism: Eleusine coracana
Primary publication:
Determination of the three-dimensional structure of the bifunctional alpha-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy.
Strobl S, Mühlhahn P, Bernstein R, Wiltscheck R, Maskos K, Wunderlich M, Huber R, Glockshuber R, Holak TA
Biochemistry 34 8281-93 (1995)
PMID: 7599120

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133933 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-amylase/trypsin inhibitor Chain: A
Molecule details ›
Chain: A
Length: 122 amino acids
Theoretical weight: 13.14 KDa
Source organism: Eleusine coracana
Expression system: Escherichia coli
UniProt:
  • Canonical: P01087 (Residues: 1-122; Coverage: 100%)
Sequence domains: Protease inhibitor/seed storage/LTP family
Structure domains: Plant lipid-transfer and hydrophobic proteins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli

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Citations

7 review citations

Plant toxic proteins with insecticidal properties. A review on their potentialities as bioinsecticides.
Carlini et al. (2002)
6 more

8 mentions without citation

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