1TMX
Crystal structure of hydroxyquinol 1,2-dioxygenase from Nocardioides Simplex 3E
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 | 0018581 | molecular_function | hydroxyquinol 1,2-dioxygenase activity |
| A | 0042952 | biological_process | beta-ketoadipate pathway |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047074 | molecular_function | 4-hydroxycatechol 1,2-dioxygenase activity |
| 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 | 0018581 | molecular_function | hydroxyquinol 1,2-dioxygenase activity |
| B | 0042952 | biological_process | beta-ketoadipate pathway |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047074 | molecular_function | 4-hydroxycatechol 1,2-dioxygenase activity |
| B | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 861 |
| Chain | Residue |
| A | TYR164 |
| A | TYR197 |
| A | HIS221 |
| A | HIS223 |
| A | BEZ881 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE B 862 |
| Chain | Residue |
| B | BEZ882 |
| B | TYR164 |
| B | TYR197 |
| B | HIS221 |
| B | HIS223 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CU A 871 |
| Chain | Residue |
| A | HIS42 |
| A | CL891 |
| B | HIS42 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 891 |
| Chain | Residue |
| A | HIS42 |
| A | CU871 |
| A | HOH1072 |
| B | HIS42 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 901 |
| Chain | Residue |
| B | THR53 |
| B | ALA55 |
| B | HOH987 |
| B | HOH1050 |
| B | HOH1112 |
| B | HOH1264 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 902 |
| Chain | Residue |
| A | LYS255 |
| A | ASP256 |
| A | SER257 |
| A | HOH941 |
| A | HOH1160 |
| A | HOH1207 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE HGX A 851 |
| Chain | Residue |
| A | PHE46 |
| A | GLY60 |
| A | PHE63 |
| A | MET208 |
| A | HOH1112 |
| B | VAL35 |
| B | HGX852 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE HGX B 852 |
| Chain | Residue |
| A | LEU32 |
| A | HGX851 |
| B | GLU56 |
| B | TRP57 |
| B | THR59 |
| B | PHE63 |
| B | ALA211 |
| B | HOH1284 |
| B | HOH1297 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE BEZ A 881 |
| Chain | Residue |
| A | LEU80 |
| A | ASP83 |
| A | GLY109 |
| A | PRO110 |
| A | PHE111 |
| A | TYR197 |
| A | ILE199 |
| A | ARG218 |
| A | HIS221 |
| A | HIS223 |
| A | FE861 |
| A | HOH908 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE BEZ B 882 |
| Chain | Residue |
| B | ASP83 |
| B | GLY109 |
| B | PRO110 |
| B | PHE111 |
| B | TYR197 |
| B | ILE199 |
| B | ARG218 |
| B | HIS221 |
| B | HIS223 |
| B | VAL251 |
| B | FE862 |
| B | HOH948 |
Functional Information from PROSITE/UniProt
| site_id | PS00083 |
| Number of Residues | 29 |
| Details | INTRADIOL_DIOXYGENAS Intradiol ring-cleavage dioxygenases signature. VeGtVtdtdGnpVpdarIEVweadddGfY |
| Chain | Residue | Details |
| A | VAL136-TYR164 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15772073 |
| Chain | Residue | Details |
| A | TYR164 | |
| A | TYR197 | |
| A | HIS221 | |
| A | HIS223 | |
| B | TYR164 | |
| B | TYR197 | |
| B | HIS221 | |
| B | HIS223 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 3pca |
| Chain | Residue | Details |
| A | ARG218 | |
| A | TYR197 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 3pca |
| Chain | Residue | Details |
| B | ARG218 | |
| B | TYR197 |
