Chaperonin 60

A group I chaperonin protein that forms the barrel-like structure of the chaperonin complex. It is an oligomeric protein with a distinctive structure of fourteen subunits, arranged in two rings of seven subunits each. The protein was originally studied in BACTERIA where it is commonly referred to as GroEL protein.

Also Known As:

GroEL Protein; GroEL Stress Protein; Heat-Shock Protein 60; hsp60 Protein; Heat Shock Protein 60; Heat Shock Proteins 60; Heat-Shock Proteins 60; hsp60 Family

Enzymes and Coenzymes: 1
- Enzymes: 152586
  - Hydrolases: 2166
    - Acid Anhydride Hydrolases
      - Adenosine Triphosphatases: 8623
        Chaperonins: 222
        Group I Chaperonins: 1
        Chaperonin 60: 509
Amino Acids, Peptides, and Proteins: 1
- Proteins: 484843
  - Molecular Chaperones: 1279
    - Heat-Shock Proteins: 8088
      - Chaperonins: 222
        Group I Chaperonins: 1
        Chaperonin 60: 509

APL-1 peptide

Bio-Agent Context: Research Results