3FGC
Crystal Structure of the Bacterial Luciferase:Flavin Complex Reveals the Basis of Intersubunit Communication
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0008218 | biological_process | bioluminescence |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0047646 | molecular_function | alkanal monooxygenase (FMN-linked) activity |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0008218 | biological_process | bioluminescence |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0047646 | molecular_function | alkanal monooxygenase (FMN-linked) activity |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0008218 | biological_process | bioluminescence |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0047646 | molecular_function | alkanal monooxygenase (FMN-linked) activity |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0008218 | biological_process | bioluminescence |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0047646 | molecular_function | alkanal monooxygenase (FMN-linked) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE FMN A 3402 |
| Chain | Residue |
| A | PHE6 |
| A | LEU109 |
| A | VAL173 |
| A | ALA174 |
| A | GLU175 |
| A | SER176 |
| A | THR179 |
| A | HOH513 |
| A | LEU42 |
| A | GLU43 |
| A | ALA74 |
| A | ALA75 |
| A | VAL77 |
| A | CYS106 |
| A | ARG107 |
| A | GLY108 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 356 |
| Chain | Residue |
| A | ARG107 |
| A | GLU175 |
| A | SER176 |
| A | THR179 |
| A | HOH513 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 357 |
| Chain | Residue |
| A | ALA146 |
| A | ASP147 |
| A | ASN148 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 358 |
| Chain | Residue |
| A | ILE151 |
| A | LYS152 |
| A | LYS274 |
| A | GLY275 |
| A | HOH366 |
| A | HOH530 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 359 |
| Chain | Residue |
| A | GLN11 |
| A | GLN17 |
| A | HOH426 |
| A | HOH539 |
| A | HOH811 |
| B | HIS161 |
| D | LYS202 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 360 |
| Chain | Residue |
| A | LYS2 |
| A | ASN70 |
| A | ARG102 |
| A | HOH483 |
| A | HOH760 |
| A | HOH761 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 361 |
| Chain | Residue |
| A | SER264 |
| A | ASP265 |
| A | HOH410 |
| B | HIS145 |
| B | PRO154 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 333 |
| Chain | Residue |
| B | LYS133 |
| B | PRO146 |
| B | ASN147 |
| B | ASN148 |
| B | HOH535 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 334 |
| Chain | Residue |
| B | SER176 |
| B | LYS177 |
| B | GLU178 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 B 335 |
| Chain | Residue |
| B | HIS145 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 356 |
| Chain | Residue |
| C | GLN11 |
| C | SER16 |
| C | GLN17 |
| C | HOH432 |
| C | HOH657 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 357 |
| Chain | Residue |
| C | LYS2 |
| C | ASN70 |
| C | ARG102 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 358 |
| Chain | Residue |
| C | ALA146 |
| C | ASP147 |
| C | ASN148 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 C 359 |
| Chain | Residue |
| C | ARG107 |
| C | VAL173 |
| C | GLU175 |
| C | SER176 |
| C | THR179 |
| C | HOH380 |
| C | HOH835 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 333 |
| Chain | Residue |
| D | LYS133 |
| D | PRO146 |
| D | ASN147 |
| D | ASN148 |
| D | HOH689 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 334 |
| Chain | Residue |
| D | GLU109 |
| D | LYS110 |
| D | SER111 |
| D | HOH827 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 335 |
| Chain | Residue |
| A | ARG278 |
| A | ASP279 |
| A | PHE280 |
| D | ARG284 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 336 |
| Chain | Residue |
| D | SER176 |
| D | LYS177 |
| D | GLU178 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 337 |
| Chain | Residue |
| D | MET1 |
| D | TYR322 |
| D | HIS323 |
Functional Information from PROSITE/UniProt
| site_id | PS00494 |
| Number of Residues | 26 |
| Details | BACTERIAL_LUCIFERASE Bacterial luciferase subunits signature. GLPLvFrWddsnaqRkeyaglYhevA |
| Chain | Residue | Details |
| B | GLY187-ALA212 | |
| A | GLY187-ALA212 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1luc |
| Chain | Residue | Details |
| A | HIS44 | |
| A | HIS45 | |
| A | PHE261 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1luc |
| Chain | Residue | Details |
| C | HIS44 | |
| C | HIS45 | |
| C | PHE261 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 132 |
| Chain | Residue | Details |
| A | HIS44 | activator, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS45 | electrostatic stabiliser, polar/non-polar interaction |
| A | CYS106 | electrostatic stabiliser |
| A | ASP113 | electrostatic stabiliser, hydrogen bond acceptor |
| A | SER227 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 132 |
| Chain | Residue | Details |
| C | HIS44 | activator, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| C | HIS45 | electrostatic stabiliser, polar/non-polar interaction |
| C | CYS106 | electrostatic stabiliser |
| C | ASP113 | electrostatic stabiliser, hydrogen bond acceptor |
| C | SER227 | electrostatic stabiliser, hydrogen bond donor |
