3P3L
Crystal Structure of the Cytochrome P450 monooxygenase AurH (wildtype) 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 | 28 |
Details | BINDING SITE FOR RESIDUE HEM A 501 |
Chain | Residue |
A | LEU90 |
A | GLN251 |
A | LEU284 |
A | THR289 |
A | LEU290 |
A | THR293 |
A | ARG296 |
A | ALA347 |
A | PHE348 |
A | GLY349 |
A | GLY350 |
A | GLN91 |
A | HIS353 |
A | CYS355 |
A | GLY357 |
A | LEU360 |
A | GLU364 |
B | HOH434 |
B | HOH441 |
B | HOH562 |
B | HOH723 |
A | HIS98 |
A | ARG102 |
A | PHE109 |
A | ALA243 |
A | GLY244 |
A | THR247 |
A | THR248 |
site_id | AC2 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE HEM B 501 |
Chain | Residue |
B | LEU90 |
B | GLN91 |
B | HIS98 |
B | ARG102 |
B | PHE109 |
B | ALA243 |
B | GLY244 |
B | THR247 |
B | THR248 |
B | LEU284 |
B | THR289 |
B | LEU290 |
B | THR293 |
B | ARG296 |
B | ALA347 |
B | PHE348 |
B | GLY349 |
B | GLY350 |
B | HIS353 |
B | CYS355 |
B | LEU356 |
B | GLY357 |
B | LEU360 |
B | ALA361 |
B | HOH615 |
B | HOH641 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 407 |
Chain | Residue |
A | ARG60 |
A | PHE223 |
A | GLY351 |
A | PRO352 |
A | EPE409 |
B | HOH529 |
B | HOH541 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 408 |
Chain | Residue |
A | ALA5 |
A | HIS6 |
A | THR7 |
B | ARG69 |
B | HOH721 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 407 |
Chain | Residue |
A | ARG69 |
B | ALA5 |
B | HIS6 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE EPE A 409 |
Chain | Residue |
A | HIS98 |
A | ARG99 |
A | ARG102 |
A | PHE223 |
A | HIS224 |
A | GLY351 |
A | PRO352 |
A | PHE354 |
A | SO4407 |
B | HOH426 |
B | HOH499 |
B | HOH736 |
site_id | AC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE EPE B 408 |
Chain | Residue |
B | HIS98 |
B | ARG99 |
B | ARG102 |
B | PHE223 |
B | HIS224 |
B | GLY351 |
B | PRO352 |
B | PHE354 |
B | HOH429 |
B | HOH717 |
B | HOH746 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 409 |
Chain | Residue |
B | ARG69 |
B | ARG112 |
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 |