Crystallization (Comment) | Organism |
---|---|
homology modeling of wild-type and mutants K259A, K259D. In the wild-type, the Lys259 residue is located close to the FAD cofactor. Lys258 makes van der Waals contacts to the ribose of FAD | Pseudomonas putida |
Protein Variants | Comment | Organism |
---|---|---|
K259A | 50% decrease in catalytic efficiency compared to wild-type | Pseudomonas putida |
K259D | 50% decrease in catalytic efficiency compared to wild-type | Pseudomonas putida |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas putida | A0A166IXY4 | - |
- |
Pseudomonas putida NBRC 14164 | A0A166IXY4 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
FprA | - |
Pseudomonas putida |
PP4_41290 | ORF name | Pseudomonas putida |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Pseudomonas putida |
General Information | Comment | Organism |
---|---|---|
physiological function | Phe256, which is important for binding to ferredoxin, and Lys259 are the crucial residues for electron transfer with ferredoxin | Pseudomonas putida |