3P3X
Crystal Structure of the Cytochrome P450 Monooxygenase AurH (nterm-AurH-I) from Streptomyces Thioluteus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0006707 | biological_process | cholesterol catabolic process |
A | 0008395 | molecular_function | steroid hydroxylase activity |
A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
A | 0020037 | molecular_function | heme binding |
A | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0006707 | biological_process | cholesterol catabolic process |
B | 0008395 | molecular_function | steroid hydroxylase activity |
B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
B | 0020037 | molecular_function | heme binding |
B | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM A 501 |
Chain | Residue |
A | GLN91 |
A | THR289 |
A | LEU290 |
A | THR293 |
A | ALA294 |
A | ARG296 |
A | ALA347 |
A | PHE348 |
A | GLY349 |
A | GLY350 |
A | PRO352 |
A | HIS98 |
A | HIS353 |
A | CYS355 |
A | GLY357 |
A | ALA361 |
A | ARG102 |
A | PHE109 |
A | VAL240 |
A | ALA243 |
A | GLY244 |
A | THR247 |
A | THR248 |
site_id | AC2 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE HEM B 501 |
Chain | Residue |
B | LEU90 |
B | GLN91 |
B | HIS98 |
B | ARG102 |
B | PHE109 |
B | VAL240 |
B | ALA243 |
B | GLY244 |
B | THR247 |
B | THR248 |
B | THR289 |
B | LEU290 |
B | THR293 |
B | ALA294 |
B | ARG296 |
B | ALA347 |
B | PHE348 |
B | GLY349 |
B | GLY350 |
B | HIS353 |
B | CYS355 |
B | LEU356 |
B | GLY357 |
B | HOH503 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 407 |
Chain | Residue |
A | GLY351 |
B | PHE223 |
B | HIS224 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 407 |
Chain | Residue |
A | LYS208 |
A | PHE223 |
A | HIS224 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 408 |
Chain | Residue |
B | PHE68 |
B | VAL292 |
B | HOH436 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 408 |
Chain | Residue |
A | ARG51 |
A | ARG327 |
B | ARG51 |
B | ARG327 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 409 |
Chain | Residue |
A | ARG99 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 409 |
Chain | Residue |
B | ARG207 |
Functional Information from PROSITE/UniProt
site_id | PS00086 |
Number of Residues | 10 |
Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGgGPHFCLG |
Chain | Residue | Details |
A | PHE348-GLY357 |