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EVIDENCE OF A COMMON DECAMER IN THREE CRYSTAL STRUCTURES OF BPTI, CRYSTALLIZE FROM THIOCYANATE, CHLORIDE OR SULFATE

X-ray diffraction
2.58Å resolution
PDB entry 1bz5 coloured by chain, front view.
PDB entry 1bz5 coloured by chain, side view.
PDB entry 1bz5 coloured by chain, top view.
Source organism: Bos taurus
Assembly composition:
homo decamer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Pancreatic trypsin inhibitor
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Multimeric state: homo decamer
Accessible surface area: 22729.41 Å2
Buried surface area: 16808.61 Å2
Dissociation area: 8,071.08 Å2
Dissociation energy (ΔGdiss): 120.4 kcal/mol
Dissociation entropy (TΔSdiss): 95.79 kcal/mol
Symmetry number: 10
PDBe Complex ID: PDB-CPX-133761
Homo decameric assembly 1 of PDB entry 1bz5 coloured by chemically distinct molecules, front view.
Homo decameric assembly 1 of PDB entry 1bz5 coloured by chemically distinct molecules, side view.
Homo decameric assembly 1 of PDB entry 1bz5 coloured by chemically distinct molecules, top view.
    Assembly 1
Confidence : 87%
No. subunits : 10
Symmetry : D5
More details
3DComplex & QSbio predictionx
No. subunits : Unclear
Symmetry : Unclear
Evidence : This biological assembly agrees with the prediction of PISA but not of EPPIC

Macromolecules

Pancreatic trypsin inhibitor
Chains: A, B, C, D, E
Length: 58 amino acids
Theoretical weight: 6.53 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00974 (Residues: 36-93; Coverage: 73%)
Pfam: Kunitz/Bovine pancreatic trypsin inhibitor domain
InterPro:
CATH: Pancreatic trypsin inhibitor Kunitz domain
SCOP: Small Kunitz-type inhibitors & BPTI-like toxins
Pancreatic trypsin inhibitor in PDB entry 1bz5, assembly 1, front view.
Pancreatic trypsin inhibitor in PDB entry 1bz5, assembly 1, side view.
Pancreatic trypsin inhibitor in PDB entry 1bz5, assembly 1, top view.
PDBe-KB: UniProt Coverage View: P00974  
158510152025303540455055
 
2040RPDFCLEPPYTGPCKARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCMRTCGGA
UniProt
P00974
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces
Sequence conservation
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