CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.60 | Sandwich |
|
2.60.34 | Substrate Binding Domain Of DNAk; Chain A, domain 1 |
|
2.60.34.10 | Substrate Binding Domain Of DNAk; Chain A, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Substrate Binding Domain Of DNAk; Chain A, domain 1 |
| Functional Family | Molecular chaperone DnaK |
Enzyme Information
| 3.6.4.10 |
Non-chaperonin molecular chaperone ATPase.
based on mapping to UniProt G3I8R9
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)
| G3I8R9 |
BIP_CRIGR
Cricetulus griseus
Endoplasmic reticulum chaperone BiP
|
PDB Structure
| PDB | 6EOB |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
AMPylation targets the rate-limiting step of BiP's ATPase cycle for its functional inactivation.
Elife
|