PDBe 4cms

X-ray diffraction
2.2Å resolution

X-RAY ANALYSES OF ASPARTIC PROTEINASES IV. STRUCTURE AND REFINEMENT AT 2.2 ANGSTROMS RESOLUTION OF BOVINE CHYMOSIN

Released:

Function and Biology Details

Reaction catalysed:
Broad specificity similar to that of pepsin A. Clots milk by cleavage of a single 104-Ser-Phe-|-Met-Ala-107 bond in kappa-chain of casein. 
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chymosin Chain: A
Molecule details ›
Chain: A
Length: 323 amino acids
Theoretical weight: 35.67 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00794 (Residues: 59-381; Coverage: 89%)
Gene names: CPC, CYM
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 79.98Å b: 114.12Å c: 72.76Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 not available not available
Expression system: Not provided