Crystallization (Comment) | Organism |
---|---|
double electron-electron resonance studies. The geometry of the complex is nearly identical for the open and closed states of P450cam. Putaredoxin makes a single distinct interaction with its binding site on the enzyme and triggers the conformational change through very subtle structural interactions | Pseudomonas putida |
Protein Variants | Comment | Organism |
---|---|---|
Q227C | mutation used for double electron-electron resonance studies | Pseudomonas putida |
Q272C | mutation used for double electron-electron resonance studies | Pseudomonas putida |
S190C | mutation used for double electron-electron resonance studies. Residues S48C and S190C are at opposite ends of the substrate access channel to provide a longer distance measurement | Pseudomonas putida |
S48C | mutation used for double electron-electron resonance studies. Residues S48C and S190C are at opposite ends of the substrate access channel to provide a longer distance measurement | Pseudomonas putida |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas putida | P00183 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
CYP101A1 | - |
Pseudomonas putida |
P450cam | - |
Pseudomonas putida |