Literature summary extracted from
Priyadarshi, A.; Kim, E.; Hwang, K.
Structural insights into Staphylococcus aureus enoyl-ACP reductase (FabI), in complex with NADP end triclosan (2010), Proteins Struct. Funct. Bioinform., 78, 480-486.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.3.1.39 |
apo-enzyme and complex with NADPH and inhibitor triclosan. Enzyme is a tetramer. In the apo-form of the SaFabI structure, residues Ile193 to Leu196 form part of a flexible loop adjacent to the active site. In the open conformation, the loop is on the surface of the protein, and does not form any secondary structure or contribute to inhibitor or cofactor binding. The substrate-binding loop of the holo-enzyme containing Ser197, Val201 and Phe204 has a closed conformation |
Staphylococcus aureus |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.3.1.39 |
triclosan |
affinity varies with pH-value |
Staphylococcus aureus |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.3.1.39 |
Staphylococcus aureus |
Q6GI75 |
- |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.3.1.39 |
FabI |
- |
Staphylococcus aureus |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.3.1.39 |
NADPH |
- |
Staphylococcus aureus |
|