CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.560 | GROEL; domain 1 |
|
1.10.560.10 | GroEL-like equatorial domain |
Domain Context
CATH Clusters
| Superfamily | GroEL-like equatorial domain |
| Functional Family | 60 kDa heat shock protein, mitochondrial |
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.
Proc.Natl.Acad.Sci.USA
|