1BPI: Bovine pancreatic trypsin inhibitor

The structure of bovine pancreatic trypsin inhibitor at 125K: definition of carboxyl-terminal residues glycine-57 and alanine-58. Determined by X-ray diffraction at 1.09 Å resolution. Released 3 Jun 1995.

Method
X-ray diffraction
Resolution
1.09 Å
Organism
Bos taurus
Chains
1
Atoms
637
Mol. weight
6.62 kDa
Ligands
PO4
Released
3 Jun 1995

Explore 1BPI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1BPI contains 3 α-helices and 3 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 3 helices, 3 β-strands

ElementResiduesLengthSheet
α-helix3-64
α-helix8-92
β-strand18-2471
β-strand29-3571
β-strand4511
α-helix48-558

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bovine pancreatic trypsin inhibitorAprotein58Bos taurusP00974 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1BPI_1 BOVINE PANCREATIC TRYPSIN INHIBITOR (chains A)
RPDFCLEPPYTGPCKARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCMRTCGGA

Ligands and cofactors

IDNameFormulaCopies
PO4Phosphate ionO4 P1

Primary citation

Structure of bovine pancreatic trypsin inhibitor at 125 K definition of carboxyl-terminal residues Gly57 and Ala58. Parkin, S., Rupp, B., Hope, H. Acta Crystallogr D Biol Crystallogr (1996) 52:18-29. DOI 10.1107/S0907444995008675 · PubMed

Other PDB entries of the same protein (UniProt P00974 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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