Literature summary extracted from
Engel, C.K.; Kiema, T.R.; Hiltunen, J.K.; Wierenga, R.K.
The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule (1998), J. Mol. Biol., 275, 847-859.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.2.1.17 |
hanging drop method, structure of the mitochondrial enoyl-CoA hydratase, co-crystallised with the inhibitor octanoyl-CoA, refined at a resolution of 2.4 A |
Rattus norvegicus |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
4.2.1.17 |
octanoyl-CoA |
- |
Rattus norvegicus |
|
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
4.2.1.17 |
mitochondrion |
- |
Rattus norvegicus |
5739 |
- |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.2.1.17 |
Rattus norvegicus |
P14604 |
the classification is ambiguous because the stereochemistry is not exactly determined |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.2.1.17 |
enoyl-CoA hydratase |
the classification is ambiguous because the stereochemistry is not exactly determined |
Rattus norvegicus |