3O32
Crystal Structure of 4-Chlorocatechol Dioxygenase from Rhodococcus opacus 1CP in complex with 3,5-dichlorocatechol
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 | 0009712 | biological_process | catechol-containing compound metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0009712 | biological_process | catechol-containing compound metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 35C258 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 35C A 258 |
| Chain | Residue |
| A | TYR134 |
| A | TYR169 |
| A | ARG191 |
| A | HIS194 |
| A | HIS196 |
| A | CYS224 |
| A | FE300 |
| A | LEU49 |
| A | ASP52 |
| A | ALA53 |
| A | GLY76 |
| A | PRO77 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MYY A 303 |
| Chain | Residue |
| A | THR33 |
| A | TYR37 |
| A | TYR184 |
| B | VAL6 |
| B | LEU9 |
| B | PHE13 |
| B | MYY304 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FE B 301 |
| Chain | Residue |
| B | HIS194 |
| B | HIS196 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MYY B 304 |
| Chain | Residue |
| A | VAL6 |
| A | LEU9 |
| A | PHE13 |
| A | MYY303 |
| B | ILE34 |
| B | TYR37 |
| B | TRP50 |
| B | TYR184 |
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 site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
