Structure analysis

STRUCTURE OF THE TRYPSIN-BINDING DOMAIN OF BOWMAN-BIRK TYPE PROTEASE INHIBITOR AND ITS INTERACTION WITH TRYPSIN

X-ray diffraction
2.3Å resolution
Source organisms:
Assembly composition:
Non-polymer only tetramer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: Non-polymer only tetramer
Accessible surface area: 20900 Å2
Buried surface area: 4100 Å2
Dissociation area: 2,100 Å2
Dissociation energy (ΔGdiss): -8 kcal/mol
Dissociation entropy (TΔSdiss): 33 kcal/mol
Interface energy (ΔGint): -7 kcal/mol
Symmetry number: 2

Macromolecules

Chain: E
Length: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
Pfam: Trypsin
InterPro:
CATH: Trypsin-like serine proteases
SCOP: Eukaryotic proteases

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Chain: I
Length: 82 amino acids
Theoretical weight: 9.14 KDa
Source organism: Vigna angularis
Expression system: Not provided
UniProt:
  • Canonical: P01058 (Residues: 1-82; Coverage: 100%)
Pfam: Bowman-Birk serine protease inhibitor family
InterPro:
SCOP: Bowman-Birk inhibitor, BBI

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