PDBe 1n8o

X-ray diffraction
2Å resolution

Crystal structure of a complex between bovine chymotrypsin and ecotin

Released:
Entry authors: Cambillau C, Spinelli S, Lauwereys M

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Ecotin Chain: E
Molecule details ›
Chain: E
Length: 142 amino acids
Theoretical weight: 16.12 KDa
Source organism: Escherichia coli K-12
UniProt:
  • Best match: P23827 (Residues: 21-162)
Gene names: JW2197, b2209, eco, eti
Chymotrypsin A chain A Chain: A
Molecule details ›
Chain: A
Length: 13 amino acids
Theoretical weight: 1.25 KDa
Source organism: Bos taurus
UniProt:
  • Best match: P00766 (Residues: 1-13)
Chymotrypsin A chain C Chain: C
Molecule details ›
Chain: C
Length: 97 amino acids
Theoretical weight: 10.07 KDa
Source organism: Bos taurus
UniProt:
  • Best match: P00766 (Residues: 149-245)
Chymotrypsin A chain B Chain: B
Molecule details ›
Chain: B
Length: 131 amino acids
Theoretical weight: 13.93 KDa
Source organism: Bos taurus
UniProt:
  • Best match: P00766 (Residues: 16-146)

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 95.5Å b: 63.8Å c: 79.6Å
α: 90° β: 91.7° γ: 90°
R-values:
R R work R free
0.205 0.205 not available