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 3A4 |
Enzyme Information
| 1.14.14.56 |
1,8-cineole 2-exo-monooxygenase.
based on mapping to UniProt P08684
1,8-cineole + [reduced NADPH--hemoprotein reductase] + O(2) = 2-exo- hydroxy-1,8-cineole + [oxidized NADPH--hemoprotein reductase] + H(2)O.
-!- The mammalian enzyme, expressed in liver microsomes, performs a variety of oxidation reactions of structurally unrelated compounds, including stereoids, fatty acids, and xenobiotics. -!- Cf. EC 1.14.14.55, EC 1.14.14.57 and EC 1.14.14.73. -!- Formerly EC 1.14.13.157.
|
| 1.14.14.55 |
Quinine 3-monooxygenase.
based on mapping to UniProt P08684
Quinine + [reduced NADPH--hemoprotein reductase] + O(2) = 3-hydroxyquinine + [oxidized NADPH--hemoprotein reductase] + H(2)O.
-!- Formerly EC 1.14.13.67.
|
| 1.14.14.- |
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen.
based on mapping to UniProt P08684
|
| 1.14.14.73 |
Albendazole monooxygenase (sufoxide-forming).
based on mapping to UniProt P08684
(1) Albendazole + [reduced NADPH--hemoprotein reductase] + O(2) = albendazole S-oxide + [oxidized NADPH--hemoprotein reductase] + H(2)O. (2) Fenbendazole + [reduced NADPH--hemoprotein reductase] + O(2) = fenbendazole S-oxide + [oxidized NADPH--hemoprotein reductase] + H(2)O.
-!- This is one of the activities carried out by some microsomal cytochrome P450 monooxygenases. -!- A similar conversion is also carried out by a different microsomal enzyme (EC 1.14.13.32), but it is estimated that cytochrome P450s are responsible for 70% of the activity.
|
UniProtKB Entries (1)
| P08684 |
CP3A4_HUMAN
Homo sapiens
Cytochrome P450 3A4
|
PDB Structure
| PDB | 6DA2 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure-Activity Relationships of Rationally Designed Ritonavir Analogues: Impact of Side-Group Stereochemistry, Headgroup Spacing, and Backbone Composition on the Interaction with CYP3A4.
Biochemistry
|
