5VQB
Crystal structure of rifampin monooxygenase from Streptomyces venezuelae, complex with FAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0006744 | biological_process | ubiquinone biosynthetic process |
| 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 | 0043719 | molecular_function | 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase activity |
| A | 0071949 | molecular_function | FAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0006744 | biological_process | ubiquinone biosynthetic process |
| 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 | 0043719 | molecular_function | 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase activity |
| B | 0071949 | molecular_function | FAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0006744 | biological_process | ubiquinone biosynthetic process |
| 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 | 0043719 | molecular_function | 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase activity |
| C | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | VAL7 |
| A | ALA42 |
| A | GLN98 |
| A | LEU122 |
| A | CYS150 |
| A | ASP151 |
| A | GLY152 |
| A | THR156 |
| A | GLY276 |
| A | ASP277 |
| A | PRO284 |
| A | GLY8 |
| A | GLN288 |
| A | GLY289 |
| A | LEU290 |
| A | ASN291 |
| A | GLY10 |
| A | PRO11 |
| A | THR12 |
| A | LEU30 |
| A | GLU31 |
| A | LYS32 |
| A | ARG41 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| A | GLU357 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 503 |
| Chain | Residue |
| A | ARG352 |
| A | HOH618 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 504 |
| Chain | Residue |
| A | ARG401 |
| C | GLU64 |
| site_id | AC5 |
| Number of Residues | 23 |
| 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 | GLN98 |
| B | LEU122 |
| B | CYS150 |
| B | ASP151 |
| B | GLY152 |
| B | THR156 |
| B | PHE257 |
| B | ASP277 |
| B | PRO284 |
| B | GLN288 |
| B | GLY289 |
| B | LEU290 |
| B | ASN291 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| A | ARG118 |
| A | ARG120 |
| B | GLU129 |
| B | ASP270 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 503 |
| Chain | Residue |
| B | ARG61 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 505 |
| Chain | Residue |
| B | GLU357 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 506 |
| Chain | Residue |
| B | ARG21 |
| site_id | AD1 |
| Number of Residues | 23 |
| Details | binding site for residue FAD C 501 |
| Chain | Residue |
| C | VAL7 |
| C | GLY8 |
| C | GLY10 |
| C | PRO11 |
| C | THR12 |
| C | LEU30 |
| C | GLU31 |
| C | LYS32 |
| C | ARG41 |
| C | ALA42 |
| C | GLN98 |
| C | LEU122 |
| C | CYS150 |
| C | ASP151 |
| C | GLY152 |
| C | THR156 |
| C | LEU176 |
| C | GLY276 |
| C | ASP277 |
| C | PRO284 |
| C | GLY289 |
| C | LEU290 |
| C | ASN291 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue CL C 502 |
| Chain | Residue |
| A | LEU112 |
| C | HIS399 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 27 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29398560, ECO:0007744|PDB:5VQB, ECO:0007744|PDB:6BRD |
| Chain | Residue | Details |
| C | ASP277 | |
| C | LEU290 | |
| C | ASN291 | |
| A | LYS32 | |
| A | GLN98 | |
| A | LEU122 | |
| A | THR156 | |
| A | ASN291 | |
| B | THR12 | |
| B | GLU31 | |
| B | LYS32 | |
| B | GLN98 | |
| B | LEU122 | |
| B | THR156 | |
| B | ASP277 | |
| B | LEU290 | |
| B | ASN291 | |
| C | THR12 | |
| C | GLU31 | |
| C | LYS32 | |
| C | GLN98 | |
| C | LEU122 | |
| C | THR156 | |
| A | ASP277 | |
| A | LEU290 | |
| A | THR12 | |
| A | GLU31 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29398560, ECO:0007744|PDB:6BRD |
| Chain | Residue | Details |
| A | ARG196 | |
| A | ARG213 | |
| B | ARG196 | |
| B | ARG213 | |
| C | ARG196 | |
| C | ARG213 |
