PDBe 4cha

X-ray diffraction
1.68Å resolution

STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION

Released:
Source organism: Bos taurus
Primary publication:
Structure of alpha-chymotrypsin refined at 1.68 A resolution.
J. Mol. Biol. 184 703-11 (1985)
PMID: 4046030

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Tyr-|-, Trp-|-, Phe-|-, Leu-|-.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Chymotrypsin A chain A Chains: A, E
Molecule details ›
Chains: A, E
Length: 13 amino acids
Theoretical weight: 1.25 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 1-13; Coverage: 5%)
Chymotrypsin A chain B Chains: B, F
Molecule details ›
Chains: B, F
Length: 131 amino acids
Theoretical weight: 13.93 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 16-146; Coverage: 54%)
Structure domains: Trypsin-like serine proteases
Chymotrypsin A chain C Chains: C, G
Molecule details ›
Chains: C, G
Length: 97 amino acids
Theoretical weight: 10.07 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 149-245; Coverage: 40%)
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 49.23Å b: 67.39Å c: 65.99Å
α: 90° β: 101.8° γ: 90°