EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.14.15.1 | 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 |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.15.1 | Q227C | mutation used for double electron-electron resonance studies | Pseudomonas putida |
1.14.15.1 | Q272C | mutation used for double electron-electron resonance studies | Pseudomonas putida |
1.14.15.1 | 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 |
1.14.15.1 | 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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.15.1 | Pseudomonas putida | P00183 | - |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.15.1 | CYP101A1 | - |
Pseudomonas putida |
1.14.15.1 | P450cam | - |
Pseudomonas putida |