CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.420 | Nucleotidyltransferase; domain 5 |
|
3.30.420.40 | ATPase, nucleotide binding domain |
Domain Context
CATH Clusters
| Superfamily | 3.30.420.40 |
| Functional Family | heat shock 70 kDa protein-like |
Enzyme Information
| 3.6.4.10 |
Non-chaperonin molecular chaperone ATPase.
based on mapping to UniProt P11021
ATP + H(2)O = ADP + phosphate.
-!- This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. -!- They comprise a number of heat-shock-cognate proteins. -!- They are also active in clathrin uncoating and in the oligomerization of actin.
|
UniProtKB Entries (1)
| P11021 |
BIP_HUMAN
Homo sapiens
Endoplasmic reticulum chaperone BiP
|
PDB Structure
| PDB | 6ASY |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s.
Nat Commun
|