Structure analysis

THE REFINED 2.0 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN BOVINE BETA-TRYPSIN AND CMTI-I, A TRYPSIN INHIBITOR FROM SQUASH SEEDS (CUCURBITA MAXIMA): TOPOLOGICAL SIMILARITY OF THE SQUASH SEED INHIBITORS WITH THE CARBOXYPEPTIDASE A INHIBITOR FROM POTATOES

X-ray diffraction
2Å resolution
Source organisms:
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 9918.74 Å2
Buried surface area: 1684.38 Å2
Dissociation area: 842.19 Å2
Dissociation energy (ΔGdiss): 5.5 kcal/mol
Dissociation entropy (TΔSdiss): 9.3 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-133328

Macromolecules

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Chain: I
Length: 29 amino acids
Theoretical weight: 3.28 KDa
Source organism: Cucurbita maxima
Expression system: Not provided
UniProt:
  • Canonical: P01074 (Residues: 1-29; Coverage: 100%)
Pfam: Squash family serine protease inhibitor
InterPro:
SCOP: Plant inhibitors of proteinases and amylases

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