CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.630 | Cytochrome p450 |
|
1.10.630.10 | Cytochrome P450 |
Domain Context
CATH Clusters
| Superfamily | Cytochrome P450 |
| Functional Family | Cytochrome P450 1A1 |
Enzyme Information
| 1.14.14.- |
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen.
based on mapping to UniProt P04798
|
| 4.2.1.152 |
Hydroperoxy icosatetraenoate dehydratase.
based on mapping to UniProt P04798
A hydroperoxy icosatetraenoate = an oxoicosatetraenoate + H(2)O.
-!- The mammalian enzymes accept a range of hydroperoxy icosatetraenoates (HPETE). -!- The human enzyme has highest activity with (12R)-HPETE, followed by (12S)-HPETE and (15R)-HPETE with much lower efficiency. -!- The murine enzyme has highest activity with (8R)-HPETE followed by (8S)-HPETE. All HPETE isoforms are converted to the corresponding oxoicosatetraenoate forms (KETE). -!- The enzymes also catalyze the reaction of EC 5.4.4.7.
|
UniProtKB Entries (1)
| P04798 |
CP1A1_HUMAN
Homo sapiens
Cytochrome P450 1A1
|
PDB Structure
| PDB | 6DWM |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structures of human cytochrome P450 1A1 with bergamottin and erlotinib reveal active-site modifications for binding of diverse ligands.
J. Biol. Chem.
|