3O6J
Crystal Structure of 4-Chlorocatechol Dioxygenase from Rhodococcus opacus 1CP in complex with hydroxyquinol
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0008199 | molecular_function | ferric iron binding |
A | 0009056 | biological_process | catabolic process |
A | 0009712 | biological_process | catechol-containing compound metabolic process |
A | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
A | 0018576 | molecular_function | catechol 1,2-dioxygenase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051213 | molecular_function | dioxygenase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0008199 | molecular_function | ferric iron binding |
B | 0009056 | biological_process | catabolic process |
B | 0009712 | biological_process | catechol-containing compound metabolic process |
B | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
B | 0018576 | molecular_function | catechol 1,2-dioxygenase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE A 300 |
Chain | Residue |
A | TYR134 |
A | HIS194 |
A | HIS196 |
A | HQN258 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MYY A 304 |
Chain | Residue |
B | TYR37 |
B | TRP50 |
B | TYR184 |
B | MYY303 |
A | ASN3 |
A | VAL6 |
A | LEU9 |
A | PHE13 |
B | ILE34 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE HQN A 258 |
Chain | Residue |
A | GLY76 |
A | PRO77 |
A | TYR134 |
A | TYR169 |
A | ARG191 |
A | HIS194 |
A | HIS196 |
A | CYS224 |
A | FE300 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 259 |
Chain | Residue |
A | GLU81 |
A | ARG150 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE B 301 |
Chain | Residue |
B | PHE78 |
B | TYR134 |
B | HIS194 |
B | HIS196 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MYY B 303 |
Chain | Residue |
A | TYR37 |
A | TRP50 |
A | TYR184 |
A | MYY304 |
B | ALA2 |
B | LEU9 |
B | PHE13 |
Functional Information from PROSITE/UniProt
site_id | PS00083 |
Number of Residues | 29 |
Details | INTRADIOL_DIOXYGENAS Intradiol ring-cleavage dioxygenases signature. FtGsVrdtsGtpItgavIDVwhstndGnY |
Chain | Residue | Details |
A | PHE106-TYR134 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | TYR134 | |
A | TYR169 | |
A | HIS194 | |
A | HIS196 | |
B | TYR134 | |
B | TYR169 | |
B | HIS194 | |
B | HIS196 |