Protein family
Protein sequence
Protein function
Catalytic activity
EC number
EC number description
1.14.14.1
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor;
unspecific monooxygenase
1.14.14.55
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor;
quinine 3-monooxygenase
1.14.14.56
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor;
1,8-cineole 2-exo-monooxygenase
1.14.14.73
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor;
albendazole monooxygenase (sulfoxide-forming)
PDB | Resolution (Å) | PDB name |
---|---|---|
1TQN | 2.05 | Crystal Structure of Human Microsomal P450 3A4 |
1W0E | 2.8 | Crystal structure of human cytochrome P450 3A4 |
1W0F | 2.65 | Crystal structure of human cytochrome P450 3A4 |
1W0G | 2.73 | Crystal structure of human cytochrome P450 3A4 |
2J0D | 2.75 | Crystal structure of human P450 3A4 in complex with erythromycin |
2V0M | 2.8 | Crystal structure of human P450 3A4 in complex with ketoconazole |
3NXU | 2.0 | Crystal structure of human cytochrome P4503A4 bound to an inhibitor ritonavir |
3TJS | 2.25 | Crystal Structure of the complex between human cytochrome P450 3A4 and desthiazolylmethyloxycarbonyl ritonavir |
3UA1 | 2.15 | Crystal structure of the cytochrome P4503A4-bromoergocryptine complex |
4D6Z | 1.93 | Cytochrome P450 3A4 bound to imidazole and an inhibitor |
4D75 | 2.25 | Cytochrome P450 3A4 bound to an inhibitor |
4D78 | 2.8 | Cytochrome P450 3A4 bound to an inhibitor |
4D7D | 2.76 | Cytochrome P450 3A4 bound to an inhibitor |
4I3Q | 2.602 | Crystal structure of human CYP3A4 coordinated to a water molecule |
4I4G | 2.718 | Crystal structure of CYP3A4 ligated to oxazole-substituted desoxyritonavir |
4I4H | 2.9 | Crystal structure of CYP3A4 ligated to pyridine-substituted desoxyritonavir |
4K9T | 2.5 | Complex of CYP3A4 with a desoxyritonavir analog |
4K9U | 2.85 | Complex of human CYP3A4 with a desoxyritonavir analog |
4K9V | 2.6 | Complex of CYP3A4 with a desoxyritonavir analog |
4K9W | 2.399 | Complex of human CYP3A4 with a desoxyritonavir analog |
4K9X | 2.76 | Complex of human CYP3A4 with a desoxyritonavir analog |
4NY4 | 2.95 | Crystal structure of CYP3A4 in complex with an inhibitor |
5A1P | 2.5 | Crystal structure of cytochrome P450 3A4 bound to progesterone and citrate |
5A1R | 2.45 | Crystal structure of cytochrome P450 3A4 bound to progesterone |
5G5J | 2.6 | Crystal structure of human CYP3A4 bound to metformin |
5TE8 | 2.7 | Crystal structure of the midazolam-bound human CYP3A4 |
5VC0 | 2.7 | Crystal structure of human CYP3A4 bound to ritonavir |
5VCC | 1.7 | Crystal structure of human CYP3A4 bound to glycerol |
5VCD | 1.95 | Crystal structure of the cysteine depleted CYP3A4 bound to glycerol |
5VCE | 2.2 | Crystal structure of the cysteine depleted CYP3A4 bound to ritonavir |
5VCG | 2.2 | Crystal structure of the cysteine depleted CYP3A4 bound to bromoergocryptine |
6BCZ | 2.23 | Crystal structure of human CYP3A4 bound to an inhibitor |
6BD5 | 2.5 | Crystal structure of human CYP3A4 bound to an inhibitor |
6BD6 | 2.5 | Crystal structure of human CYP3A4 bound to an inhibitor |
6BD7 | 2.42 | Crystal structure of human CYP3A4 bound to an inhibitor |
6BD8 | 2.38 | Crystal structure of human CYP3A4 bound to an inhibitor |
6BDH | 2.25 | Crystal structure of human CYP3A4 bound to an inhibitor |
6BDI | 2.57 | Crystal structure of human CYP3A4 bound to an inhibitor |
6BDK | 2.67 | Crystal structure of human CYP3A4 bound to an inhibitor |
6BDM | 2.6 | Crystal structure of human CYP3A4 bound to an inhibitor |
6OO9 | 2.25 | Human CYP3A4 bound to a drug mibefradil |
6OOA | 2.52 | Human CYP3A4 bound to a drug substrate |
6OOB | 2.202 | Human CYP3A4 bound to a suicide substrate |
7KS8 | 2.5 | Crystal structure of human CYP3A4 with the caged inhibitor |
7KSA | 2.5 | Crystal structure of human CYP3A4 with the caged inhibitor |
7KVH | 2.791 | Human CYP3A4 bound to an inhibitor |
7KVI | 2.55 | Human CYP3A4 bound to an inhibitor |
7KVJ | 2.65 | Human CYP3A4 bound to an inhibitor |
7KVK | 2.55 | Human CYP3A4 bound to an inhibitor |
7KVM | 2.75 | Human CYP3A4 bound to an inhibitor |
7KVN | 2.7 | Human CYP3A4 bound to an inhibitor |
7KVO | 2.65 | Human CYP3A4 bound to an inhibitor |
7KVP | 2.75 | Human CYP3A4 bound to an inhibitor |
7KVQ | 2.75 | Human CYP3A4 bound to an inhibitor |
7KVS | 2.5 | Human CYP3A4 bound to an inhibitor |
7LXL | 2.75 | Crystal structure of human CYP3A4 bound to the testosterone dimer |
7UAY | 2.78 | Crystal structure of human CYP3A4 with the caged inhibitor |
7UAZ | 2.65 | Crystal structure of human CYP3A4 with the caged inhibitor |
7UF9 | 2.45 | CYP3A4 bound to an inhibitor |
7UFA | 2.5 | CYP3A4 bound to an inhibitor |
7UFB | 2.25 | CYP3A4 bound to an inhibitor |
7UFC | 2.35 | Human CYP3A4 bound to an inhibitor |
7UFD | 2.9 | Human CYP3A4 bound to an inhibitor |
7UFE | 2.4 | Human CYP3A4 bound to an inhibitor |
7UFF | 2.7 | Human CYP3A4 bound to an inhibitor |
8DYC | 2.4 | Human CYP3A4 bound to a substrate |
8EWD | 2.2 | Crystal structure of CYP3A4 bound to an inhibitor |
8EWE | 2.3 | Crystal structure of CYP3A4 bound to an inhibitor |
8EWL | 2.35 | Crystal structure of CYP3A4 bound to an inhibitor |
8EWM | 2.3 | Crystal structure of CYP3A4 bound to an inhibitor |
8EWN | 2.1 | Crystal structure of CYP3A4 bound to an inhibitor |
8EWP | 2.4 | Crystal structure of CYP3A4 bound to an inhibitor |
8EWQ | 2.25 | Crystal structure of CYP3A4 bound to an inhibitor |
8EWR | 2.2 | Crystal structure of CYP3A4 bound to an inhibitor |
8EWS | 2.15 | Crystal structure of CYP3A4 bound to an inhibitor |
8EXB | 2.05 | Crystal structure of CYP3A4 bound to an inhibitor |
GO ontology | GO term | GO description |
---|---|---|
Biological Process | GO:0046222 | aflatoxin metabolic process |
Biological Process | GO:0009822 | alkaloid catabolic process |
Biological Process | GO:0008209 | androgen metabolic process |
Biological Process | GO:0008203 | cholesterol metabolic process |
Biological Process | GO:0008210 | estrogen metabolic process |
Biological Process | GO:0046483 | heterocycle metabolic process |
Biological Process | GO:0002933 | lipid hydroxylation |
Biological Process | GO:0006629 | lipid metabolic process |
Biological Process | GO:0042759 | long-chain fatty acid biosynthetic process |
Biological Process | GO:0016098 | monoterpenoid metabolic process |
Biological Process | GO:0070989 | oxidative demethylation |
Biological Process | GO:0042573 | retinoic acid metabolic process |
Biological Process | GO:0042572 | retinol metabolic process |
Biological Process | GO:0006706 | steroid catabolic process |
Biological Process | GO:0008202 | steroid metabolic process |
Biological Process | GO:0042369 | vitamin D catabolic process |
Biological Process | GO:0042359 | vitamin D metabolic process |
Biological Process | GO:0042178 | xenobiotic catabolic process |
Biological Process | GO:0006805 | xenobiotic metabolic process |
Molecular Function | GO:0102320 | 1,8-cineole 2-exo-monooxygenase activity |
Molecular Function | GO:0062181 | 1-alpha,25-dihydroxyvitamin D3 23-hydroxylase activity |
Molecular Function | GO:0062188 | anandamide 11,12 epoxidase activity |
Molecular Function | GO:0062189 | anandamide 14,15 epoxidase activity |
Molecular Function | GO:0062187 | anandamide 8,9 epoxidase activity |
Molecular Function | GO:0070330 | aromatase activity |
Molecular Function | GO:0034875 | caffeine oxidase activity |
Molecular Function | GO:0019899 | enzyme binding |
Molecular Function | GO:0101020 | estrogen 16-alpha-hydroxylase activity |
Molecular Function | GO:0101021 | estrogen 2-hydroxylase activity |
Molecular Function | GO:0020037 | heme binding |
Molecular Function | GO:0005506 | iron ion binding |
Molecular Function | GO:0004497 | monooxygenase activity |
Molecular Function | GO:0016491 | oxidoreductase activity |
Molecular Function | GO:0019825 | oxygen binding |
Molecular Function | GO:0050591 | quinine 3-monooxygenase activity |
Molecular Function | GO:0008401 | retinoic acid 4-hydroxylase activity |
Molecular Function | GO:0005496 | steroid binding |
Molecular Function | GO:0008395 | steroid hydroxylase activity |
Molecular Function | GO:0050649 | testosterone 6-beta-hydroxylase activity |
Molecular Function | GO:0070576 | vitamin D 24-hydroxylase activity |
Molecular Function | GO:0030343 | vitamin D3 25-hydroxylase activity |
Cellular Component | GO:0005737 | cytoplasm |
Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
Cellular Component | GO:0043231 | intracellular membrane-bounded organelle |
Reactome | Reactome Name | Node type | Reactome Root | Reactome Root Name |
---|---|---|---|---|
R-HSA-211945 | Phase I - Functionalization of compounds | Internal node | R-HSA-1430728 | Metabolism |
R-HSA-211981 | Xenobiotics | Internal node | R-HSA-1430728 | Metabolism |
R-HSA-5423646 | Aflatoxin activation and detoxification | Leaf | R-HSA-1430728 | Metabolism |
R-HSA-9027307 | Biosynthesis of maresin-like SPMs | Leaf | R-HSA-1430728 | Metabolism |
R-HSA-9749641 | Aspirin ADME | Leaf | R-HSA-9748784 | Drug ADME |
R-HSA-9754706 | Atorvastatin ADME | Leaf | R-HSA-9748784 | Drug ADME |
R-HSA-9757110 | Prednisone ADME | Leaf | R-HSA-9748784 | Drug ADME |
Location | ECO term | Pubmed |
---|---|---|
Endoplasmic reticulum membrane | ||
Microsome membrane | ECO:0000269 | PubMed:21576599 |
HPO ID | HPO name |
---|---|
HP:0000006 | Autosomal dominant inheritance |
HP:0000938 | Osteopenia |
HP:0001510 | Growth delay |
HP:0002148 | Hypophosphatemia |
HP:0002901 | Hypocalcemia |
HP:0002970 | Genu varum |
HP:0002979 | Bowing of the legs |
HP:0003015 | Flared metaphysis |
HP:0003021 | Metaphyseal cupping |
HP:0003155 | Elevated circulating alkaline phosphatase concentration |
HP:0003165 | Elevated circulating parathyroid hormone level |
HP:0011463 | Childhood onset |
HP:0012052 | Low serum calcitriol |
HP:0012053 | Decreased circulating calcifediol concentration |
HP:0031936 | Delayed ability to walk |
Disease name | MONDO ID | ICD10 | ICD10 chapter | OMIM | Orphanet |
---|---|---|---|---|---|
vitamin d-dependent rickets- type 3 | MONDO:0033640 | E83 | chapter4, Endocrine, nutritional and metabolic diseases | OMIM:619073 |