6ZGP
Crystal structure of the quaternary ammonium Rieske monooxygenase CntA in complex with inhibitor MMV12 (MMV020670)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0009437 | biological_process | carnitine metabolic 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 | 0044237 | biological_process | cellular metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0009437 | biological_process | carnitine metabolic 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 | 0044237 | biological_process | cellular metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051213 | molecular_function | dioxygenase activity |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0009437 | biological_process | carnitine metabolic 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 | 0044237 | biological_process | cellular metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051213 | molecular_function | dioxygenase activity |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0009437 | biological_process | carnitine metabolic process |
| D | 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 |
| D | 0044237 | biological_process | cellular metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051213 | molecular_function | dioxygenase activity |
| D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| E | 0004497 | molecular_function | monooxygenase activity |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0009437 | biological_process | carnitine metabolic process |
| E | 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 |
| E | 0044237 | biological_process | cellular metabolic process |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051213 | molecular_function | dioxygenase activity |
| E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| F | 0004497 | molecular_function | monooxygenase activity |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0009437 | biological_process | carnitine metabolic process |
| F | 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 |
| F | 0044237 | biological_process | cellular metabolic process |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051213 | molecular_function | dioxygenase activity |
| F | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| G | 0004497 | molecular_function | monooxygenase activity |
| G | 0005506 | molecular_function | iron ion binding |
| G | 0009437 | biological_process | carnitine metabolic process |
| G | 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 |
| G | 0044237 | biological_process | cellular metabolic process |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0051213 | molecular_function | dioxygenase activity |
| G | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| H | 0004497 | molecular_function | monooxygenase activity |
| H | 0005506 | molecular_function | iron ion binding |
| H | 0009437 | biological_process | carnitine metabolic process |
| H | 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 |
| H | 0044237 | biological_process | cellular metabolic process |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0051213 | molecular_function | dioxygenase activity |
| H | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| I | 0004497 | molecular_function | monooxygenase activity |
| I | 0005506 | molecular_function | iron ion binding |
| I | 0009437 | biological_process | carnitine metabolic process |
| I | 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 |
| I | 0044237 | biological_process | cellular metabolic process |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0051213 | molecular_function | dioxygenase activity |
| I | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| J | 0004497 | molecular_function | monooxygenase activity |
| J | 0005506 | molecular_function | iron ion binding |
| J | 0009437 | biological_process | carnitine metabolic process |
| J | 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 |
| J | 0044237 | biological_process | cellular metabolic process |
| J | 0046872 | molecular_function | metal ion binding |
| J | 0051213 | molecular_function | dioxygenase activity |
| J | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| K | 0004497 | molecular_function | monooxygenase activity |
| K | 0005506 | molecular_function | iron ion binding |
| K | 0009437 | biological_process | carnitine metabolic process |
| K | 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 |
| K | 0044237 | biological_process | cellular metabolic process |
| K | 0046872 | molecular_function | metal ion binding |
| K | 0051213 | molecular_function | dioxygenase activity |
| K | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| L | 0004497 | molecular_function | monooxygenase activity |
| L | 0005506 | molecular_function | iron ion binding |
| L | 0009437 | biological_process | carnitine metabolic process |
| L | 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 |
| L | 0044237 | biological_process | cellular metabolic process |
| L | 0046872 | molecular_function | metal ion binding |
| L | 0051213 | molecular_function | dioxygenase activity |
| L | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue FE A 401 |
| Chain | Residue |
| A | HIS208 |
| A | HIS213 |
| A | ASP323 |
| A | QKQ403 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue FES A 402 |
| Chain | Residue |
| A | HIS109 |
| A | CYS86 |
| A | HIS88 |
| A | ARG89 |
| A | HIS91 |
| A | CYS106 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue QKQ A 403 |
| Chain | Residue |
| A | TYR203 |
| A | HIS213 |
| A | PHE216 |
| A | TYR225 |
| A | GLN236 |
| A | PHE258 |
| A | HIS259 |
| A | GLY260 |
| A | ASN270 |
| A | PRO272 |
| A | PRO273 |
| A | THR279 |
| A | TYR295 |
| A | TYR315 |
| A | PHE319 |
| A | ASP323 |
| A | FE401 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EPE A 404 |
| Chain | Residue |
| A | PHE11 |
| A | TRP19 |
| A | ARG340 |
| A | GLN342 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue FE B 401 |
| Chain | Residue |
| B | HIS208 |
| B | HIS213 |
| B | ASP323 |
| B | QKQ403 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue FES B 402 |
| Chain | Residue |
| B | CYS86 |
| B | HIS88 |
| B | ARG89 |
| B | CYS106 |
| B | TYR108 |
| B | HIS109 |
| B | TRP111 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | binding site for residue QKQ B 403 |
| Chain | Residue |
| B | TYR203 |
| B | GLU205 |
| B | CYS206 |
| B | HIS208 |
| B | PHE216 |
| B | TYR225 |
| B | GLN236 |
| B | PHE258 |
| B | HIS259 |
| B | GLY260 |
| B | ASN270 |
| B | PRO272 |
| B | PRO273 |
| B | THR279 |
| B | TYR295 |
| B | TYR315 |
| B | PHE319 |
| B | ASP323 |
| B | FE401 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EPE B 404 |
| Chain | Residue |
| B | TRP19 |
| B | ARG340 |
| B | GLY341 |
| B | GLN342 |
| B | HOH527 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue FE C 401 |
| Chain | Residue |
| C | HIS208 |
| C | HIS213 |
| C | ASP323 |
| C | QKQ403 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue FES C 402 |
| Chain | Residue |
| C | CYS86 |
| C | HIS88 |
| C | ARG89 |
| C | CYS106 |
| C | HIS109 |
| C | TRP111 |
| site_id | AD2 |
| Number of Residues | 17 |
| Details | binding site for residue QKQ C 403 |
| Chain | Residue |
| C | CYS206 |
| C | HIS208 |
| C | PHE216 |
| C | TYR225 |
| C | GLN236 |
| C | PHE258 |
| C | HIS259 |
| C | GLY260 |
| C | ASN270 |
| C | PRO272 |
| C | PRO273 |
| C | THR279 |
| C | TYR295 |
| C | TYR315 |
| C | PHE319 |
| C | ASP323 |
| C | FE401 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue EPE C 404 |
| Chain | Residue |
| C | TRP19 |
| C | ARG340 |
| C | GLN342 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue FE D 401 |
| Chain | Residue |
| D | QKQ403 |
| D | HIS208 |
| D | HIS213 |
| D | ASP323 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue FES D 402 |
| Chain | Residue |
| D | CYS86 |
| D | HIS88 |
| D | ARG89 |
| D | HIS91 |
| D | CYS106 |
| D | TYR108 |
| D | HIS109 |
| D | TRP111 |
| site_id | AD6 |
| Number of Residues | 18 |
| Details | binding site for residue QKQ D 403 |
| Chain | Residue |
| D | TYR203 |
| D | GLU205 |
| D | CYS206 |
| D | PHE216 |
| D | TYR225 |
| D | GLN236 |
| D | PHE258 |
| D | HIS259 |
| D | GLY260 |
| D | ASN270 |
| D | PRO272 |
| D | PRO273 |
| D | THR279 |
| D | TYR295 |
| D | TYR315 |
| D | PHE319 |
| D | ASP323 |
| D | FE401 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue EPE D 404 |
| Chain | Residue |
| D | PHE11 |
| D | TRP19 |
| D | ARG340 |
| D | GLN342 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue FE E 401 |
| Chain | Residue |
| E | HIS208 |
| E | HIS213 |
| E | ASP323 |
| E | QKQ403 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for residue FES E 402 |
| Chain | Residue |
| E | CYS86 |
| E | HIS88 |
| E | ARG89 |
| E | CYS106 |
| E | TYR108 |
| E | HIS109 |
| E | TRP111 |
| site_id | AE1 |
| Number of Residues | 19 |
| Details | binding site for residue QKQ E 403 |
| Chain | Residue |
| E | TYR203 |
| E | GLU205 |
| E | CYS206 |
| E | HIS208 |
| E | HIS213 |
| E | PHE216 |
| E | TYR225 |
| E | GLN236 |
| E | PHE258 |
| E | HIS259 |
| E | GLY260 |
| E | ASN270 |
| E | PRO272 |
| E | THR279 |
| E | TYR295 |
| E | TYR315 |
| E | PHE319 |
| E | ASP323 |
| E | FE401 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue EPE E 404 |
| Chain | Residue |
| E | TRP19 |
| E | ARG340 |
| E | GLN342 |
| E | HOH560 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue FE F 401 |
| Chain | Residue |
| F | HIS208 |
| F | HIS213 |
| F | ASP323 |
| F | QKQ403 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue FES F 402 |
| Chain | Residue |
| F | CYS86 |
| F | HIS88 |
| F | ARG89 |
| F | CYS106 |
| F | HIS109 |
| F | TRP111 |
| site_id | AE5 |
| Number of Residues | 18 |
| Details | binding site for residue QKQ F 403 |
| Chain | Residue |
| F | CYS206 |
| F | PHE216 |
| F | SER219 |
| F | TYR225 |
| F | GLN236 |
| F | PHE258 |
| F | HIS259 |
| F | GLY260 |
| F | ASN270 |
| F | PRO272 |
| F | PRO273 |
| F | THR279 |
| F | TYR295 |
| F | TYR315 |
| F | PHE319 |
| F | ASP323 |
| F | FE401 |
| F | HOH612 |
| site_id | AE6 |
| Number of Residues | 5 |
| Details | binding site for residue EPE F 404 |
| Chain | Residue |
| F | TRP19 |
| F | ARG340 |
| F | GLY341 |
| F | GLN342 |
| F | HOH513 |
| site_id | AE7 |
| Number of Residues | 4 |
| Details | binding site for residue FE G 401 |
| Chain | Residue |
| G | HIS208 |
| G | HIS213 |
| G | ASP323 |
| G | QKQ403 |
| site_id | AE8 |
| Number of Residues | 6 |
| Details | binding site for residue FES G 402 |
| Chain | Residue |
| G | CYS86 |
| G | HIS88 |
| G | ARG89 |
| G | CYS106 |
| G | HIS109 |
| G | TRP111 |
| site_id | AE9 |
| Number of Residues | 21 |
| Details | binding site for residue QKQ G 403 |
| Chain | Residue |
| G | TYR203 |
| G | GLU205 |
| G | CYS206 |
| G | HIS208 |
| G | HIS213 |
| G | PHE216 |
| G | TYR225 |
| G | GLN236 |
| G | PHE247 |
| G | PHE258 |
| G | HIS259 |
| G | GLY260 |
| G | ASN270 |
| G | PRO272 |
| G | PRO273 |
| G | THR279 |
| G | TYR295 |
| G | TYR315 |
| G | PHE319 |
| G | ASP323 |
| G | FE401 |
| site_id | AF1 |
| Number of Residues | 5 |
| Details | binding site for residue EPE G 404 |
| Chain | Residue |
| G | PHE11 |
| G | TRP19 |
| G | ARG340 |
| G | GLN342 |
| G | HOH552 |
| site_id | AF2 |
| Number of Residues | 4 |
| Details | binding site for residue FE H 401 |
| Chain | Residue |
| H | HIS208 |
| H | HIS213 |
| H | ASP323 |
| H | QKQ403 |
| site_id | AF3 |
| Number of Residues | 6 |
| Details | binding site for residue FES H 402 |
| Chain | Residue |
| H | CYS86 |
| H | HIS88 |
| H | ARG89 |
| H | CYS106 |
| H | HIS109 |
| H | TRP111 |
| site_id | AF4 |
| Number of Residues | 18 |
| Details | binding site for residue QKQ H 403 |
| Chain | Residue |
| H | TYR203 |
| H | GLU205 |
| H | CYS206 |
| H | HIS208 |
| H | TYR225 |
| H | GLN236 |
| H | PHE258 |
| H | HIS259 |
| H | GLY260 |
| H | ASN270 |
| H | PRO272 |
| H | PRO273 |
| H | THR279 |
| H | TYR295 |
| H | TYR315 |
| H | PHE319 |
| H | ASP323 |
| H | FE401 |
| site_id | AF5 |
| Number of Residues | 4 |
| Details | binding site for residue EPE H 404 |
| Chain | Residue |
| H | PHE11 |
| H | TRP19 |
| H | ARG340 |
| H | GLN342 |
| site_id | AF6 |
| Number of Residues | 4 |
| Details | binding site for residue FE I 401 |
| Chain | Residue |
| I | HIS208 |
| I | HIS213 |
| I | ASP323 |
| I | QKQ403 |
| site_id | AF7 |
| Number of Residues | 6 |
| Details | binding site for residue FES I 402 |
| Chain | Residue |
| I | CYS86 |
| I | HIS88 |
| I | ARG89 |
| I | CYS106 |
| I | HIS109 |
| I | TRP111 |
| site_id | AF8 |
| Number of Residues | 15 |
| Details | binding site for residue QKQ I 403 |
| Chain | Residue |
| I | TYR203 |
| I | CYS206 |
| I | PHE216 |
| I | TYR225 |
| I | GLN236 |
| I | PHE258 |
| I | HIS259 |
| I | ASN270 |
| I | PRO272 |
| I | THR279 |
| I | TYR295 |
| I | TYR315 |
| I | PHE319 |
| I | ASP323 |
| I | FE401 |
| site_id | AF9 |
| Number of Residues | 4 |
| Details | binding site for residue EPE I 404 |
| Chain | Residue |
| I | PHE11 |
| I | TRP19 |
| I | ARG340 |
| I | GLN342 |
| site_id | AG1 |
| Number of Residues | 5 |
| Details | binding site for residue FE J 401 |
| Chain | Residue |
| J | ASN202 |
| J | HIS208 |
| J | HIS213 |
| J | ASP323 |
| J | QKQ403 |
| site_id | AG2 |
| Number of Residues | 7 |
| Details | binding site for residue FES J 402 |
| Chain | Residue |
| J | CYS86 |
| J | HIS88 |
| J | ARG89 |
| J | HIS91 |
| J | CYS106 |
| J | TYR108 |
| J | HIS109 |
| site_id | AG3 |
| Number of Residues | 20 |
| Details | binding site for residue QKQ J 403 |
| Chain | Residue |
| J | ASN202 |
| J | TYR203 |
| J | GLU205 |
| J | CYS206 |
| J | HIS208 |
| J | PHE216 |
| J | VAL220 |
| J | TYR225 |
| J | GLN236 |
| J | PHE258 |
| J | HIS259 |
| J | GLY260 |
| J | ASN270 |
| J | PRO273 |
| J | THR279 |
| J | TYR295 |
| J | TYR315 |
| J | PHE319 |
| J | ASP323 |
| J | FE401 |
| site_id | AG4 |
| Number of Residues | 4 |
| Details | binding site for residue EPE J 404 |
| Chain | Residue |
| J | TRP19 |
| J | ARG340 |
| J | GLN342 |
| J | HOH524 |
| site_id | AG5 |
| Number of Residues | 4 |
| Details | binding site for residue FE K 401 |
| Chain | Residue |
| K | HIS208 |
| K | HIS213 |
| K | ASP323 |
| K | QKQ403 |
| site_id | AG6 |
| Number of Residues | 7 |
| Details | binding site for residue FES K 402 |
| Chain | Residue |
| K | CYS86 |
| K | HIS88 |
| K | ARG89 |
| K | CYS106 |
| K | TYR108 |
| K | HIS109 |
| K | TRP111 |
| site_id | AG7 |
| Number of Residues | 16 |
| Details | binding site for residue QKQ K 403 |
| Chain | Residue |
| K | TYR203 |
| K | GLU205 |
| K | CYS206 |
| K | TYR225 |
| K | GLN236 |
| K | PHE258 |
| K | HIS259 |
| K | GLY260 |
| K | ASN270 |
| K | PRO272 |
| K | THR279 |
| K | TYR295 |
| K | TYR315 |
| K | PHE319 |
| K | ASP323 |
| K | FE401 |
| site_id | AG8 |
| Number of Residues | 3 |
| Details | binding site for residue EPE K 404 |
| Chain | Residue |
| K | TRP19 |
| K | ARG340 |
| K | GLN342 |
| site_id | AG9 |
| Number of Residues | 4 |
| Details | binding site for residue FE L 401 |
| Chain | Residue |
| L | HIS208 |
| L | HIS213 |
| L | ASP323 |
| L | QKQ403 |
| site_id | AH1 |
| Number of Residues | 7 |
| Details | binding site for residue FES L 402 |
| Chain | Residue |
| L | CYS86 |
| L | HIS88 |
| L | ARG89 |
| L | CYS106 |
| L | TYR108 |
| L | HIS109 |
| L | TRP111 |
| site_id | AH2 |
| Number of Residues | 17 |
| Details | binding site for residue QKQ L 403 |
| Chain | Residue |
| L | TYR203 |
| L | CYS206 |
| L | PHE216 |
| L | TYR225 |
| L | GLN236 |
| L | PHE258 |
| L | HIS259 |
| L | GLY260 |
| L | ASN270 |
| L | PRO272 |
| L | PRO273 |
| L | THR279 |
| L | TYR295 |
| L | TYR315 |
| L | PHE319 |
| L | ASP323 |
| L | FE401 |
| site_id | AH3 |
| Number of Residues | 4 |
| Details | binding site for residue EPE L 404 |
| Chain | Residue |
| L | TRP19 |
| L | ARG340 |
| L | GLN342 |
| L | HOH516 |
Functional Information from PROSITE/UniProt
| site_id | PS00570 |
| Number of Residues | 24 |
| Details | RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CpHRGhellsgsgKAknvitCpYH |
| Chain | Residue | Details |
| A | CYS86-HIS109 |
