6Y9D
Crystal structure of the quaternary ammonium Rieske monooxygenase CntA in complex with substrate L-Carnitine
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 | 5 |
| Details | binding site for residue FE A 401 |
| Chain | Residue |
| A | HIS208 |
| A | HIS213 |
| A | ASP323 |
| A | SCN404 |
| A | HOH535 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue FES A 402 |
| Chain | Residue |
| A | TYR108 |
| A | HIS109 |
| A | TRP111 |
| A | CYS86 |
| A | HIS88 |
| A | ARG89 |
| A | CYS106 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue 152 A 403 |
| Chain | Residue |
| A | TYR203 |
| A | GLU205 |
| A | CYS206 |
| A | GLN236 |
| A | PHE258 |
| A | ASN270 |
| A | TYR295 |
| A | PHE319 |
| A | SCN404 |
| A | HOH542 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue SCN A 404 |
| Chain | Residue |
| A | CYS209 |
| A | HIS213 |
| A | PHE216 |
| A | PHE319 |
| A | ASP323 |
| A | FE401 |
| A | 152403 |
| A | HOH535 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EPE A 405 |
| Chain | Residue |
| A | ARG340 |
| A | GLY341 |
| A | GLN342 |
| A | HOH556 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue FE B 401 |
| Chain | Residue |
| B | HIS208 |
| B | HIS213 |
| B | ASP323 |
| B | SCN404 |
| B | HOH562 |
| site_id | AC7 |
| 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 | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue 152 B 403 |
| Chain | Residue |
| B | TYR203 |
| B | GLU205 |
| B | GLN236 |
| B | PHE258 |
| B | ASN270 |
| B | TYR295 |
| B | PHE319 |
| B | SCN404 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue SCN B 404 |
| Chain | Residue |
| B | CYS209 |
| B | HIS213 |
| B | PHE319 |
| B | ASP323 |
| B | FE401 |
| B | 152403 |
| B | HOH562 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue EPE B 405 |
| Chain | Residue |
| B | TRP19 |
| B | GLN342 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue FE C 401 |
| Chain | Residue |
| C | HIS208 |
| C | HIS213 |
| C | ASP323 |
| C | SCN404 |
| C | HOH532 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue FES C 402 |
| Chain | Residue |
| C | CYS86 |
| C | HIS88 |
| C | ARG89 |
| C | CYS106 |
| C | TYR108 |
| C | HIS109 |
| C | TRP111 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue 152 C 403 |
| Chain | Residue |
| C | TYR203 |
| C | GLU205 |
| C | CYS206 |
| C | GLN236 |
| C | ASN270 |
| C | TYR295 |
| C | PHE319 |
| C | SCN404 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue SCN C 404 |
| Chain | Residue |
| C | HIS208 |
| C | CYS209 |
| C | PHE216 |
| C | FE401 |
| C | 152403 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue EPE C 405 |
| Chain | Residue |
| C | PHE11 |
| C | TRP19 |
| C | ARG340 |
| C | GLN342 |
| C | HOH552 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue FE D 401 |
| Chain | Residue |
| D | HIS208 |
| D | HIS213 |
| D | ASP323 |
| D | SCN404 |
| D | HOH540 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue FES D 402 |
| Chain | Residue |
| D | HIS88 |
| D | ARG89 |
| D | CYS106 |
| D | HIS109 |
| D | TRP111 |
| D | CYS86 |
| site_id | AD9 |
| Number of Residues | 11 |
| Details | binding site for residue 152 D 403 |
| Chain | Residue |
| D | TYR203 |
| D | GLU205 |
| D | CYS206 |
| D | GLN236 |
| D | PHE258 |
| D | ASN270 |
| D | TYR295 |
| D | PHE319 |
| D | SCN404 |
| D | HOH522 |
| D | HOH533 |
| site_id | AE1 |
| Number of Residues | 7 |
| Details | binding site for residue SCN D 404 |
| Chain | Residue |
| D | CYS209 |
| D | HIS213 |
| D | PHE216 |
| D | PHE319 |
| D | ASP323 |
| D | FE401 |
| D | 152403 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue EPE D 405 |
| Chain | Residue |
| D | PHE11 |
| D | TRP19 |
| D | ARG340 |
| D | GLN342 |
| site_id | AE3 |
| Number of Residues | 5 |
| Details | binding site for residue FE E 401 |
| Chain | Residue |
| E | HIS208 |
| E | HIS213 |
| E | ASP323 |
| E | SCN404 |
| E | HOH552 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue FES E 402 |
| Chain | Residue |
| E | CYS86 |
| E | HIS88 |
| E | CYS106 |
| E | TYR108 |
| E | HIS109 |
| E | TRP111 |
| site_id | AE5 |
| Number of Residues | 10 |
| Details | binding site for residue 152 E 403 |
| Chain | Residue |
| E | TYR203 |
| E | GLU205 |
| E | CYS206 |
| E | GLN236 |
| E | PHE258 |
| E | ASN270 |
| E | TYR295 |
| E | PHE319 |
| E | SCN404 |
| E | HOH549 |
| site_id | AE6 |
| Number of Residues | 6 |
| Details | binding site for residue SCN E 404 |
| Chain | Residue |
| E | CYS209 |
| E | HIS213 |
| E | PHE319 |
| E | ASP323 |
| E | FE401 |
| E | 152403 |
| site_id | AE7 |
| Number of Residues | 5 |
| Details | binding site for residue EPE E 405 |
| Chain | Residue |
| E | PHE11 |
| E | TRP19 |
| E | ARG340 |
| E | GLY341 |
| E | GLN342 |
| site_id | AE8 |
| Number of Residues | 5 |
| Details | binding site for residue FE F 401 |
| Chain | Residue |
| F | HIS208 |
| F | HIS213 |
| F | ASP323 |
| F | SCN404 |
| F | HOH567 |
| site_id | AE9 |
| 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 | AF1 |
| Number of Residues | 11 |
| Details | binding site for residue 152 F 403 |
| Chain | Residue |
| F | TYR203 |
| F | GLU205 |
| F | CYS206 |
| F | GLN236 |
| F | PHE258 |
| F | ASN270 |
| F | TYR295 |
| F | PHE319 |
| F | SCN404 |
| F | HOH535 |
| F | HOH549 |
| site_id | AF2 |
| Number of Residues | 8 |
| Details | binding site for residue SCN F 404 |
| Chain | Residue |
| F | HIS208 |
| F | CYS209 |
| F | HIS213 |
| F | PHE216 |
| F | PHE319 |
| F | ASP323 |
| F | FE401 |
| F | 152403 |
| site_id | AF3 |
| Number of Residues | 4 |
| Details | binding site for residue EPE F 405 |
| Chain | Residue |
| E | ASN135 |
| F | TRP19 |
| F | GLN342 |
| F | HOH546 |
| site_id | AF4 |
| Number of Residues | 5 |
| Details | binding site for residue FE G 401 |
| Chain | Residue |
| G | HIS208 |
| G | HIS213 |
| G | ASP323 |
| G | SCN404 |
| G | HOH535 |
| site_id | AF5 |
| 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 | AF6 |
| Number of Residues | 9 |
| Details | binding site for residue 152 G 403 |
| Chain | Residue |
| G | TYR203 |
| G | GLU205 |
| G | CYS206 |
| G | GLN236 |
| G | PHE258 |
| G | ASN270 |
| G | TYR295 |
| G | SCN404 |
| G | HOH506 |
| site_id | AF7 |
| Number of Residues | 8 |
| Details | binding site for residue SCN G 404 |
| Chain | Residue |
| G | HIS208 |
| G | HIS213 |
| G | PHE216 |
| G | PHE319 |
| G | ASP323 |
| G | FE401 |
| G | 152403 |
| G | HOH535 |
| site_id | AF8 |
| Number of Residues | 5 |
| Details | binding site for residue EPE G 405 |
| Chain | Residue |
| G | PHE11 |
| G | TRP19 |
| G | ARG340 |
| G | GLN342 |
| G | HOH543 |
| site_id | AF9 |
| Number of Residues | 5 |
| Details | binding site for residue FE H 401 |
| Chain | Residue |
| H | HIS208 |
| H | HIS213 |
| H | ASP323 |
| H | SCN404 |
| H | HOH571 |
| site_id | AG1 |
| Number of Residues | 7 |
| Details | binding site for residue FES H 402 |
| Chain | Residue |
| H | CYS86 |
| H | HIS88 |
| H | ARG89 |
| H | CYS106 |
| H | TYR108 |
| H | HIS109 |
| H | TRP111 |
| site_id | AG2 |
| Number of Residues | 12 |
| Details | binding site for residue 152 H 403 |
| Chain | Residue |
| H | TYR203 |
| H | GLU205 |
| H | CYS206 |
| H | TYR225 |
| H | GLN236 |
| H | PHE258 |
| H | ASN270 |
| H | TYR295 |
| H | PHE319 |
| H | SCN404 |
| H | HOH554 |
| H | HOH566 |
| site_id | AG3 |
| Number of Residues | 6 |
| Details | binding site for residue SCN H 404 |
| Chain | Residue |
| H | HIS208 |
| H | CYS209 |
| H | HIS213 |
| H | PHE216 |
| H | FE401 |
| H | 152403 |
| site_id | AG4 |
| Number of Residues | 4 |
| Details | binding site for residue EPE H 405 |
| Chain | Residue |
| H | TRP19 |
| H | ARG340 |
| H | GLN342 |
| H | HOH537 |
| site_id | AG5 |
| Number of Residues | 5 |
| Details | binding site for residue FE I 401 |
| Chain | Residue |
| I | HIS208 |
| I | HIS213 |
| I | ASP323 |
| I | SCN404 |
| I | HOH571 |
| site_id | AG6 |
| 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 | AG7 |
| Number of Residues | 10 |
| Details | binding site for residue 152 I 403 |
| Chain | Residue |
| I | TYR203 |
| I | GLU205 |
| I | CYS206 |
| I | GLN236 |
| I | PHE258 |
| I | ASN270 |
| I | TYR295 |
| I | PHE319 |
| I | SCN404 |
| I | HOH550 |
| site_id | AG8 |
| Number of Residues | 6 |
| Details | binding site for residue SCN I 404 |
| Chain | Residue |
| I | HIS213 |
| I | PHE216 |
| I | PHE319 |
| I | FE401 |
| I | 152403 |
| I | HOH571 |
| site_id | AG9 |
| Number of Residues | 4 |
| Details | binding site for residue EPE I 405 |
| Chain | Residue |
| I | TRP19 |
| I | ARG340 |
| I | GLN342 |
| I | HOH547 |
| site_id | AH1 |
| Number of Residues | 5 |
| Details | binding site for residue FE J 401 |
| Chain | Residue |
| J | HIS208 |
| J | HIS213 |
| J | ASP323 |
| J | SCN404 |
| J | HOH519 |
| site_id | AH2 |
| Number of Residues | 6 |
| Details | binding site for residue FES J 402 |
| Chain | Residue |
| J | CYS86 |
| J | HIS88 |
| J | ARG89 |
| J | CYS106 |
| J | HIS109 |
| J | TRP111 |
| site_id | AH3 |
| Number of Residues | 10 |
| Details | binding site for residue 152 J 403 |
| Chain | Residue |
| J | TYR203 |
| J | GLU205 |
| J | CYS206 |
| J | GLN236 |
| J | PHE258 |
| J | ASN270 |
| J | TYR295 |
| J | PHE319 |
| J | SCN404 |
| J | HOH516 |
| site_id | AH4 |
| Number of Residues | 5 |
| Details | binding site for residue SCN J 404 |
| Chain | Residue |
| J | CYS209 |
| J | HIS213 |
| J | PHE319 |
| J | FE401 |
| J | 152403 |
| site_id | AH5 |
| Number of Residues | 4 |
| Details | binding site for residue EPE J 405 |
| Chain | Residue |
| J | PHE11 |
| J | TRP19 |
| J | GLN342 |
| J | HOH514 |
| site_id | AH6 |
| Number of Residues | 5 |
| Details | binding site for residue FE K 401 |
| Chain | Residue |
| K | HIS208 |
| K | HIS213 |
| K | ASP323 |
| K | SCN404 |
| K | HOH534 |
| site_id | AH7 |
| 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 | AH8 |
| Number of Residues | 11 |
| Details | binding site for residue 152 K 403 |
| Chain | Residue |
| K | TYR203 |
| K | GLU205 |
| K | CYS206 |
| K | TYR225 |
| K | GLN236 |
| K | PHE258 |
| K | ASN270 |
| K | TYR295 |
| K | PHE319 |
| K | SCN404 |
| K | HOH532 |
| site_id | AH9 |
| Number of Residues | 8 |
| Details | binding site for residue SCN K 404 |
| Chain | Residue |
| K | HIS208 |
| K | CYS209 |
| K | HIS213 |
| K | PHE216 |
| K | PHE319 |
| K | FE401 |
| K | 152403 |
| K | HOH534 |
| site_id | AI1 |
| Number of Residues | 4 |
| Details | binding site for residue EPE K 405 |
| Chain | Residue |
| K | TRP19 |
| K | ARG340 |
| K | GLN342 |
| K | HOH545 |
| site_id | AI2 |
| Number of Residues | 5 |
| Details | binding site for residue FE L 401 |
| Chain | Residue |
| L | HIS208 |
| L | HIS213 |
| L | ASP323 |
| L | SCN404 |
| L | HOH543 |
| site_id | AI3 |
| Number of Residues | 6 |
| Details | binding site for residue FES L 402 |
| Chain | Residue |
| L | CYS86 |
| L | HIS88 |
| L | ARG89 |
| L | CYS106 |
| L | HIS109 |
| L | TRP111 |
| site_id | AI4 |
| Number of Residues | 9 |
| Details | binding site for residue 152 L 403 |
| Chain | Residue |
| L | TYR203 |
| L | GLU205 |
| L | CYS206 |
| L | GLN236 |
| L | ASN270 |
| L | TYR295 |
| L | PHE319 |
| L | SCN404 |
| L | HOH522 |
| site_id | AI5 |
| Number of Residues | 7 |
| Details | binding site for residue SCN L 404 |
| Chain | Residue |
| L | HIS208 |
| L | HIS213 |
| L | PHE216 |
| L | PHE319 |
| L | FE401 |
| L | 152403 |
| L | HOH543 |
| site_id | AI6 |
| Number of Residues | 3 |
| Details | binding site for residue EPE L 405 |
| Chain | Residue |
| L | TRP19 |
| L | ARG340 |
| L | GLN342 |
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 |
