6BRD
Crystal structure of rifampin monooxygenase from Streptomyces venezuelae, complexed with rifampin and FAD
Replaces: 5VQCFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| A | 0071949 | molecular_function | FAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| B | 0071949 | molecular_function | FAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| C | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | VAL7 |
| A | ALA42 |
| A | GLN43 |
| A | GLN98 |
| A | ARG120 |
| A | ALA121 |
| A | LEU122 |
| A | CYS150 |
| A | ASP151 |
| A | GLY152 |
| A | THR156 |
| A | GLY8 |
| A | LEU176 |
| A | PHE257 |
| A | ASP277 |
| A | PRO284 |
| A | GLY287 |
| A | GLY289 |
| A | LEU290 |
| A | ASN291 |
| A | RFP502 |
| A | GLY10 |
| A | PRO11 |
| A | THR12 |
| A | GLU31 |
| A | LYS32 |
| A | GLU33 |
| A | ARG41 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue RFP A 502 |
| Chain | Residue |
| A | GLN43 |
| A | HIS46 |
| A | VAL69 |
| A | PHE74 |
| A | ARG196 |
| A | ARG201 |
| A | ALA204 |
| A | MET205 |
| A | ARG213 |
| A | VAL215 |
| A | THR285 |
| A | GLY286 |
| A | MET342 |
| A | FAD501 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 503 |
| Chain | Residue |
| A | GLU357 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 504 |
| Chain | Residue |
| A | ARG158 |
| A | LYS159 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 505 |
| Chain | Residue |
| A | HIS108 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 506 |
| Chain | Residue |
| B | ARG336 |
| site_id | AC7 |
| Number of Residues | 27 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | VAL7 |
| B | GLY8 |
| B | GLY10 |
| B | PRO11 |
| B | THR12 |
| B | LEU30 |
| B | GLU31 |
| B | LYS32 |
| B | ARG41 |
| B | ALA42 |
| B | GLN43 |
| B | GLN98 |
| B | ARG120 |
| B | LEU122 |
| B | CYS150 |
| B | ASP151 |
| B | GLY152 |
| B | THR156 |
| B | LEU176 |
| B | PHE257 |
| B | ASP277 |
| B | PRO284 |
| B | GLY287 |
| B | GLY289 |
| B | LEU290 |
| B | ASN291 |
| B | RFP502 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | binding site for residue RFP B 502 |
| Chain | Residue |
| B | GLN43 |
| B | HIS46 |
| B | PHE74 |
| B | ARG196 |
| B | GLY203 |
| B | MET205 |
| B | ARG213 |
| B | VAL215 |
| B | PRO284 |
| B | THR285 |
| B | GLY286 |
| B | MET342 |
| B | FAD501 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 503 |
| Chain | Residue |
| B | GLY119 |
| B | GLY119 |
| B | ARG120 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 504 |
| Chain | Residue |
| B | ARG352 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 505 |
| Chain | Residue |
| B | ARG158 |
| B | VAL163 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 506 |
| Chain | Residue |
| A | HOH613 |
| B | GLU129 |
| B | HOH605 |
| B | HOH616 |
| site_id | AD4 |
| Number of Residues | 31 |
| Details | binding site for residue FAD C 501 |
| Chain | Residue |
| C | GLY9 |
| C | GLY10 |
| C | PRO11 |
| C | THR12 |
| C | LEU30 |
| C | GLU31 |
| C | LYS32 |
| C | GLU33 |
| C | ARG41 |
| C | ALA42 |
| C | GLN43 |
| C | GLN98 |
| C | ARG120 |
| C | LEU122 |
| C | CYS150 |
| C | ASP151 |
| C | GLY152 |
| C | THR156 |
| C | LEU176 |
| C | PHE257 |
| C | GLY276 |
| C | ASP277 |
| C | PRO284 |
| C | GLY287 |
| C | GLN288 |
| C | GLY289 |
| C | LEU290 |
| C | ASN291 |
| C | RFP502 |
| C | VAL7 |
| C | GLY8 |
| site_id | AD5 |
| Number of Residues | 13 |
| Details | binding site for residue RFP C 502 |
| Chain | Residue |
| C | GLN43 |
| C | VAL69 |
| C | PHE74 |
| C | VAL93 |
| C | ARG196 |
| C | GLY203 |
| C | ALA204 |
| C | MET205 |
| C | ARG213 |
| C | PRO284 |
| C | THR285 |
| C | GLY286 |
| C | FAD501 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue CL C 503 |
| Chain | Residue |
| C | ARG61 |
| C | HIS108 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue CL C 505 |
| Chain | Residue |
| C | HIS407 |
| C | HOH612 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 27 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29398560","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5VQB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BRD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29398560","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BRD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
