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 |