CATH Classification

Domain Context

CATH Clusters

Superfamily GroEL
Functional Family 60 kDa chaperonin

Enzyme Information

5.6.1.7
Chaperonin ATPase.
based on mapping to UniProt P10809
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.
-!- Multisubunit proteins with 2x7 (Type I, in most cells) or 2x8 (Type II, in Archaea) ATP-binding sites involved in maintaining an unfolded polypeptide structure before folding or entry into mitochondria and chloroplasts. -!- Molecular masses of subunits ranges from 10-90 kDa. -!- They are a subclass of molecular chaperones that are related to EC 5.6.1.5. -!- Formerly EC 3.6.4.9.

UniProtKB Entries (1)

P10809
CH60_HUMAN
Homo sapiens
60 kDa heat shock protein, mitochondrial

PDB Structure

PDB 4PJ1
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure of the human mitochondrial chaperonin symmetrical football complex.
Nisemblat, S., Yaniv, O., Parnas, A., Frolow, F., Azem, A.
Proc.Natl.Acad.Sci.USA