› 1cms

X-ray diffraction
2.3Å resolution

THE THREE-DIMENSIONAL STRUCTURE OF RECOMBINANT BOVINE CHYMOSIN AT 2.3 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1cms/pdb
PDB entry 1cms coloured by chain, front view.
PDB entry 1cms coloured by chain, side view.
PDB entry 1cms coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
The three-dimensional structure of recombinant bovine chymosin at 2.3 A resolution.
Gilliland GL, Winborne EL, Nachman J, Wlodawer A
Proteins 8 82-101 (1990)
PMID: 2217166

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.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133556 (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: 72.7Å b: 80.3Å c: 114.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 not available not available
Expression system: Not provided

Quick links

Citations

6 review citations

The structure and function of Saccharomyces cerevisiae proteinase A.
Parr et al. (2007)
5 more

5 mentions without citation

Pepsin-like aspartic proteases (PAPs) as model systems for combining biomolecular simulation with biophysical experiments.
Bhakat S. (2021)
4 more