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Literature summary extracted from
- Nucleotide-dependent conformational changes in HisP: Molecular dynamics simulations of an ABC transporter nucleotide-binding domain (2004), Biophys. J., 87, 3703-3715.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 7.4.2.1 | additional information | conformational changes within HisP that are dependent on the presence of ATP in the binding pocket of the protein, changes are predominantely confined to the alpha-helical subdomain, considerable conformational flexibility in a conserved glutamine-containing loop | Salmonella enterica subsp. enterica serovar Typhimurium |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.4.2.1 | Mg2+ | conformational changes within HisP are sensitive to the presence/absence of Mg ions bound to the ATP | Salmonella enterica subsp. enterica serovar Typhimurium |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.4.2.1 | Salmonella enterica subsp. enterica serovar Typhimurium | - |
- |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.4.2.1 | HisP | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
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Release 2023.1 (January 2023)
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