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 | 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 | 0005829 | cellular_component | cytosol |
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 | 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 | 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 |