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 | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0020037 | molecular_function | heme binding |
| 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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21280577","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3P3L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3P3O","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21280577","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3P3L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3P3O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3P3X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"21280577","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3P3L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3P3O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3P3X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
