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Literature summary for 7.4.2.3 extracted from
- Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate (2009), Proc. Natl. Acad. Sci. USA, 106, 8471-8476.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | DnaK comprises two main domains: a 44-kDa N-terminal nucleotide-binding domain that contains ATPase activity, and a 25-kDa substrate-binding domain that harbors the substrate-binding site. NMR structure determination and analysis of wild-type,full-length DnaK, complexed with the peptide NRLLLTG and with ADP, using NMR residual dipolar coupling and spin labeling methods in aqueous solution based on available crystal structures of the domains, overview | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DnaK chaperone | - |
Escherichia coli |
| Hsp70 chaperone | - |
Escherichia coli |
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Release 2023.1 (January 2023)
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