Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
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 | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
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 | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
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 | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
D | 0020037 | molecular_function | heme binding |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE HEM A 500 |
Chain | Residue |
A | ARG67 |
A | PRO300 |
A | VAL304 |
A | ARG306 |
A | LEU329 |
A | GLY356 |
A | PHE357 |
A | GLY358 |
A | ILE361 |
A | HIS362 |
A | CYS364 |
A | LEU98 |
A | LEU365 |
A | ALA370 |
A | IMD501 |
A | HOH1216 |
A | HOH1283 |
A | HOH1317 |
A | HIS106 |
A | ARG110 |
A | PHE117 |
A | ALA254 |
A | GLY255 |
A | THR258 |
A | THR259 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IMD A 501 |
Chain | Residue |
A | ALA254 |
A | GLU257 |
A | THR258 |
A | PHE403 |
A | HEM500 |
site_id | AC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM B 500 |
Chain | Residue |
B | ARG67 |
B | LEU98 |
B | HIS106 |
B | ARG110 |
B | PHE117 |
B | ALA254 |
B | GLY255 |
B | THR258 |
B | THR259 |
B | PRO300 |
B | ARG306 |
B | LEU329 |
B | GLY356 |
B | PHE357 |
B | GLY358 |
B | ILE361 |
B | HIS362 |
B | CYS364 |
B | LEU365 |
B | GLY366 |
B | ALA370 |
B | IMD501 |
B | HOH1282 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE IMD B 501 |
Chain | Residue |
B | ALA254 |
B | GLU257 |
B | THR258 |
B | HEM500 |
site_id | AC5 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM C 500 |
Chain | Residue |
C | ARG67 |
C | HIS106 |
C | ARG110 |
C | PHE117 |
C | HIS250 |
C | ALA254 |
C | GLY255 |
C | THR258 |
C | THR259 |
C | PRO300 |
C | ARG306 |
C | LEU329 |
C | GLY356 |
C | PHE357 |
C | GLY358 |
C | ILE361 |
C | HIS362 |
C | CYS364 |
C | LEU365 |
C | GLY366 |
C | ALA370 |
C | IMD501 |
C | HOH1224 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IMD C 501 |
Chain | Residue |
C | ALA254 |
C | GLU257 |
C | THR258 |
C | PHE403 |
C | HEM500 |
site_id | AC7 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEM D 500 |
Chain | Residue |
D | ILE361 |
D | HIS362 |
D | CYS364 |
D | LEU365 |
D | GLY366 |
D | IMD501 |
D | HOH1243 |
D | ARG67 |
D | HIS106 |
D | ARG110 |
D | LEU251 |
D | ALA254 |
D | THR258 |
D | THR259 |
D | MET295 |
D | PRO300 |
D | ARG306 |
D | LEU329 |
D | GLY356 |
D | PHE357 |
D | GLY358 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IMD D 501 |
Chain | Residue |
D | ALA254 |
D | GLU257 |
D | THR258 |
D | PHE403 |
D | HEM500 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO D 1201 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 1202 |
Chain | Residue |
A | GLU292 |
A | ALA351 |
A | ARG371 |
A | EDO1203 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 1203 |
Chain | Residue |
A | ARG349 |
A | ALA351 |
A | EDO1202 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO B 1204 |
Chain | Residue |
B | GLU169 |
B | GLU170 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO B 1205 |
Chain | Residue |
B | PRO288 |
B | ALA351 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 1206 |
Chain | Residue |
B | LEU11 |
B | MET12 |
B | GLY13 |
B | TRP14 |
B | ASP399 |
B | MET401 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 1207 |
Chain | Residue |
C | ALA289 |
C | GLU292 |
C | ALA351 |
C | HOH1251 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO D 1208 |
Chain | Residue |
D | ALA181 |
D | GLU184 |
D | ARG198 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 1209 |
Chain | Residue |
A | LEU359 |
A | HOH1241 |
B | ARG145 |
B | ASP412 |
B | HOH1278 |
Functional Information from PROSITE/UniProt
site_id | PS00086 |
Number of Residues | 10 |
Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGlGIHYCLG |
Chain | Residue | Details |
A | PHE357-GLY366 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1akd |
Chain | Residue | Details |
A | GLU257 | |
A | THR258 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1akd |
Chain | Residue | Details |
B | GLU257 | |
B | THR258 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1akd |
Chain | Residue | Details |
C | GLU257 | |
C | THR258 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1akd |
Chain | Residue | Details |
D | GLU257 | |
D | THR258 | |