6FSH
Crystal structure of hybrid P450 OxyBtei(BC/FGvan)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0020037 | molecular_function | heme binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
B | 0016757 | molecular_function | glycosyltransferase activity |
B | 0020037 | molecular_function | heme binding |
B | 0046872 | molecular_function | metal ion binding |
C | 0004497 | molecular_function | monooxygenase activity |
C | 0005506 | molecular_function | iron ion binding |
C | 0005515 | molecular_function | protein binding |
C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
C | 0016757 | molecular_function | glycosyltransferase activity |
C | 0020037 | molecular_function | heme binding |
C | 0046872 | molecular_function | metal ion binding |
D | 0004497 | molecular_function | monooxygenase activity |
D | 0005506 | molecular_function | iron ion binding |
D | 0005515 | molecular_function | protein binding |
D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
D | 0016757 | molecular_function | glycosyltransferase activity |
D | 0020037 | molecular_function | heme binding |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | binding site for residue HEM A 401 |
Chain | Residue |
A | LEU88 |
A | THR287 |
A | ARG289 |
A | LEU312 |
A | ALA339 |
A | PHE340 |
A | GLY341 |
A | HIS345 |
A | CYS347 |
A | GLY349 |
A | THR353 |
A | HIS96 |
A | ARG100 |
A | LEU152 |
A | ALA236 |
A | GLY237 |
A | ASN240 |
A | MET244 |
A | PRO286 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue K A 402 |
Chain | Residue |
A | TYR284 |
A | ARG383 |
A | THR384 |
A | SER385 |
A | THR386 |
A | ALA388 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue K A 403 |
Chain | Residue |
A | LEU235 |
A | ASP238 |
A | ASP239 |
site_id | AC4 |
Number of Residues | 23 |
Details | binding site for residue HEM B 401 |
Chain | Residue |
B | LEU88 |
B | MET89 |
B | HIS96 |
B | ARG100 |
B | LEU152 |
B | LEU155 |
B | ALA236 |
B | GLY237 |
B | ASN240 |
B | MET244 |
B | PRO283 |
B | PRO286 |
B | THR287 |
B | ARG289 |
B | ALA339 |
B | PHE340 |
B | GLY341 |
B | ILE344 |
B | HIS345 |
B | CYS347 |
B | GLY349 |
B | THR353 |
B | HOH521 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue K B 402 |
Chain | Residue |
A | PRO376 |
B | ARG100 |
B | HIS346 |
B | CYS347 |
site_id | AC6 |
Number of Residues | 22 |
Details | binding site for residue HEM C 401 |
Chain | Residue |
C | LEU88 |
C | MET89 |
C | HIS96 |
C | ARG100 |
C | LEU152 |
C | LEU155 |
C | ALA236 |
C | GLY237 |
C | ASN240 |
C | MET244 |
C | PRO283 |
C | PRO286 |
C | THR287 |
C | ARG289 |
C | ALA339 |
C | PHE340 |
C | GLY341 |
C | HIS345 |
C | CYS347 |
C | GLY349 |
C | THR353 |
C | HOH521 |
site_id | AC7 |
Number of Residues | 23 |
Details | binding site for residue HEM D 401 |
Chain | Residue |
D | HOH519 |
D | LEU88 |
D | MET89 |
D | HIS96 |
D | ARG100 |
D | LEU152 |
D | LEU155 |
D | ALA236 |
D | GLY237 |
D | ASN240 |
D | VAL241 |
D | MET244 |
D | PRO283 |
D | PRO286 |
D | THR287 |
D | ARG289 |
D | ALA339 |
D | PHE340 |
D | GLY341 |
D | HIS345 |
D | CYS347 |
D | GLY349 |
D | THR353 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue ACT D 402 |
Chain | Residue |
C | PRO136 |
D | HIS337 |
D | HIS342 |
Functional Information from PROSITE/UniProt