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 cognate 71 kDa protein |
Enzyme Information
| 3.6.4.10 |
Non-chaperonin molecular chaperone ATPase.
based on mapping to UniProt P16474
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)
| P16474 |
BIP_YEAST
Saccharomyces cerevisiae S288C
Endoplasmic reticulum chaperone BiP
|
PDB Structure
| PDB | 3QML |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor.
Biochem.J.
|
