4EJI
Human Cytochrome P450 2A13 in complex with two molecules of 4-(methylnitrosamino)-1-(3-puridyl)-1-butanone
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0008389 | molecular_function | coumarin 7-hydroxylase activity |
| A | 0008392 | molecular_function | arachidonic acid epoxygenase activity |
| A | 0009804 | biological_process | coumarin metabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0016712 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
| A | 0019373 | biological_process | epoxygenase P450 pathway |
| A | 0020037 | molecular_function | heme binding |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0046222 | biological_process | aflatoxin metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070330 | molecular_function | aromatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | ARG101 |
| A | PRO431 |
| A | PHE432 |
| A | SER433 |
| A | ARG437 |
| A | CYS439 |
| A | PHE440 |
| A | GLY441 |
| A | 0QA503 |
| A | VAL116 |
| A | ALA117 |
| A | ARG128 |
| A | ALA301 |
| A | GLY302 |
| A | THR305 |
| A | HIS372 |
| A | LEU395 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 0QA A 502 |
| Chain | Residue |
| A | GLN104 |
| A | PHE107 |
| A | THR212 |
| A | GLY369 |
| A | ALA371 |
| A | PHE392 |
| A | PHE480 |
| A | 0QA503 |
| A | HOH624 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 0QA A 503 |
| Chain | Residue |
| A | PHE107 |
| A | PHE111 |
| A | PHE118 |
| A | ASN297 |
| A | ALA301 |
| A | THR305 |
| A | LEU370 |
| A | HEM501 |
| A | 0QA502 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FSiGKRYCFG |
| Chain | Residue | Details |
| A | PHE432-GLY441 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN297 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | CYS439 |
