1Z03
2-Oxoquinoline 8-Monooxygenase Component: Active site Modulation by Rieske-[2fe-2S] Center Oxidation/Reduction
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| E | 0004497 | molecular_function | monooxygenase activity |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| F | 0004497 | molecular_function | monooxygenase activity |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0046872 | molecular_function | metal ion binding |
| F | 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 501 |
| Chain | Residue |
| A | HIS221 |
| A | HIS225 |
| A | ASP365 |
| A | HOH5232 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE B 501 |
| Chain | Residue |
| B | HIS221 |
| B | HIS225 |
| B | ASP365 |
| B | HOH5212 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE C 501 |
| Chain | Residue |
| C | HIS225 |
| C | ASP365 |
| C | HOH5192 |
| C | HIS221 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE D 501 |
| Chain | Residue |
| D | HIS221 |
| D | HIS225 |
| D | ASP365 |
| D | HOH5241 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE E 501 |
| Chain | Residue |
| E | HIS221 |
| E | HIS225 |
| E | ASP365 |
| E | HOH5166 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE F 501 |
| Chain | Residue |
| F | HIS221 |
| F | HIS225 |
| F | ASP365 |
| F | HOH5205 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES A 500 |
| Chain | Residue |
| A | CYS84 |
| A | HIS86 |
| A | ARG87 |
| A | CYS105 |
| A | HIS108 |
| A | PHE110 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OCH A 4600 |
| Chain | Residue |
| A | GLY216 |
| A | TYR292 |
| A | LEU302 |
| A | VAL304 |
| A | TRP307 |
| A | GLN314 |
| A | PHE361 |
| A | HOH4676 |
| A | HOH4754 |
| A | HOH5232 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES B 500 |
| Chain | Residue |
| B | CYS84 |
| B | HIS86 |
| B | ARG87 |
| B | CYS105 |
| B | HIS108 |
| B | GLY109 |
| B | PHE110 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OCH B 4601 |
| Chain | Residue |
| B | GLY216 |
| B | TYR292 |
| B | LEU302 |
| B | VAL304 |
| B | TRP307 |
| B | GLN314 |
| B | PHE361 |
| B | HOH4679 |
| B | HOH4768 |
| B | HOH5212 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES C 500 |
| Chain | Residue |
| C | CYS84 |
| C | HIS86 |
| C | ARG87 |
| C | CYS105 |
| C | HIS108 |
| C | GLY109 |
| C | PHE110 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OCH C 4602 |
| Chain | Residue |
| C | GLY216 |
| C | TYR292 |
| C | LEU302 |
| C | VAL304 |
| C | TRP307 |
| C | GLN314 |
| C | PHE361 |
| C | HOH4730 |
| C | HOH4735 |
| C | HOH5192 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES D 500 |
| Chain | Residue |
| D | CYS84 |
| D | HIS86 |
| D | ARG87 |
| D | CYS105 |
| D | HIS108 |
| D | GLY109 |
| D | PHE110 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE OCH D 4603 |
| Chain | Residue |
| D | GLY216 |
| D | TYR292 |
| D | LEU302 |
| D | VAL304 |
| D | TRP307 |
| D | GLN314 |
| D | PHE361 |
| D | HOH4702 |
| D | HOH4709 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES E 500 |
| Chain | Residue |
| E | CYS84 |
| E | HIS86 |
| E | ARG87 |
| E | CYS105 |
| E | HIS108 |
| E | GLY109 |
| E | PHE110 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE OCH E 4604 |
| Chain | Residue |
| E | LEU302 |
| E | VAL304 |
| E | TRP307 |
| E | GLN314 |
| E | PHE361 |
| E | HOH4663 |
| E | HOH4709 |
| E | GLY216 |
| E | TYR292 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES F 500 |
| Chain | Residue |
| F | CYS84 |
| F | HIS86 |
| F | ARG87 |
| F | CYS105 |
| F | HIS108 |
| F | GLY109 |
| F | PHE110 |
| site_id | BC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OCH F 4605 |
| Chain | Residue |
| F | GLY216 |
| F | TYR292 |
| F | LEU302 |
| F | VAL304 |
| F | TRP307 |
| F | GLN314 |
| F | PHE361 |
| F | HOH4721 |
| F | HOH4779 |
| F | HOH5205 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| A | HIS221 | |
| A | ASP218 | |
| C | HIS108 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| A | HIS108 | |
| B | HIS221 | |
| B | ASP218 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| C | HIS221 | |
| C | ASP218 | |
| B | HIS108 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| F | HIS108 | |
| D | HIS221 | |
| D | ASP218 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| D | HIS108 | |
| E | HIS221 | |
| E | ASP218 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| F | HIS221 | |
| F | ASP218 | |
| E | HIS108 |
