1BHC

BOVINE PANCREATIC TRYPSIN INHIBITOR CRYSTALLIZED FROM THIOCYANATE

Summary for 1BHC

• Entry DOI: 10.2210/pdb1bhc/pdb
• Descriptor: BOVINE PANCREATIC TRYPSIN INHIBITOR, THIOCYANATE ION (3 entities in total)
• Functional Keywords: protease inhibitor, trypsin
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted: P00974
• Total number of polymer chains: 10
• Total formula weight: 65856.50

Authors

Hamiaux, C.,Prange, T. (deposition date: 1998-06-05, release date: 1998-09-16, Last modification date: 2024-10-30)

Primary citation

Hamiaux, C.,Prange, T.,Ries-Kautt, M.,Ducruix, A.,Lafont, S.,Astier, J.P.,Veesler, S.
The decameric structure of bovine pancreatic trypsin inhibitor (BPTI) crystallized from thiocyanate at 2.7 A resolution.
Acta Crystallogr.,Sect.D, 55:103-113, 1999

PubMed Abstract: The structure of a monoclinic form of bovine pancreatic trypsin inhibitor (BPTI) crystallized from a thiocyanate solution has been determined and refined at 2.7 A resolution. The space group is P21 with a = 71.56, b = 73.83, c = 64.47 A, beta = 93.9 degrees and Z = 20. The ten independent molecules were located by a multi-body molecular-replacement search as developed in the AMoRe program, starting from a single monomer model (PDB code: 6PTI). The molecular arrangement of the subunits is a decamer resulting from the combination of two orthogonal fivefold and twofold non-crystallographic axes. This builds a globular micelle-like particle which minimizes hydrophobic interactions with the solvent. The refinement was conducted with non-crystallographic symmetry constraints up to a final residual of R = 0.20 (Rfree= 0.26). The root-mean-square deviations from ideal geometry were 0.015 A and 1.6 degrees on bond distances and bond angles, respectively. Several sites for thiocyanate ions were analyzed.

PubMed: 10089400
DOI: 10.1107/S0907444998008725

Experimental method

X-RAY DIFFRACTION (2.7 Å)