› 1bhc

X-ray diffraction
2.7Å resolution

BOVINE PANCREATIC TRYPSIN INHIBITOR CRYSTALLIZED FROM THIOCYANATE

Released:
DOI: 10.2210/pdb1bhc/pdb
PDB 1bhc coloured by chain and viewed from the front.
PDB 1bhc coloured by chain and viewed from the side.
PDB 1bhc coloured by chain and viewed from the top.
Source organism: Bos taurus
Primary publication:
The decameric structure of bovine pancreatic trypsin inhibitor (BPTI) crystallized from thiocyanate at 2.7 A resolution.
Hamiaux C, Prangé T, Riès-Kautt M, Ducruix A, Lafont S, Astier JP, Veesler S
Acta Crystallogr. D Biol. Crystallogr. 55 103-13 (1999)
PMID: 10089400

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pancreatic trypsin inhibitor Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 58 amino acids
Theoretical weight: 6.53 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00974 (Residues: 36-93; Coverage: 73%)
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain

Ligands and Environments

1 bound ligand:
Ligand SCN 10 x SCN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P21
Unit cell:
a: 71.56Å b: 73.83Å c: 64.47Å
α: 90° β: 93.91° γ: 90°
R-values:
R R work R free
0.201 0.201 0.265

Quick links

Citations

2 review citations

Suppression and dissolution of amyloid aggregates using ionic liquids.
Takekiyo et al. (2018)
1 more

2 mentions without citation

Protein self-association in solution: the bovine pancreatic trypsin inhibitor decamer.
Gottschalk et al. (2003)
1 more