1BRL
THREE-DIMENSIONAL STRUCTURE OF BACTERIAL LUCIFERASE FROM VIBRIO HARVEYI AT 2.4 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0008218 | biological_process | bioluminescence |
| 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 | 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 | 0008218 | biological_process | bioluminescence |
| 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 | 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 | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 356 |
| Chain | Residue |
| A | ARG107 |
| A | VAL173 |
| A | GLU175 |
| A | SER176 |
| A | THR179 |
| A | HOH2010 |
Functional Information from PROSITE/UniProt
| site_id | PS00494 |
| Number of Residues | 26 |
| Details | BACTERIAL_LUCIFERASE Bacterial luciferase subunits signature. GLPMiLsWiintheKkaqldlYnevA |
| Chain | Residue | Details |
| A | GLY187-ALA212 | |
| B | 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 |
