6D3M
FT_T dioxygenase with bound quizalofop
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000908 | molecular_function | taurine dioxygenase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006790 | biological_process | sulfur compound metabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019439 | biological_process | obsolete aromatic compound catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0051213 | molecular_function | dioxygenase activity |
B | 0000908 | molecular_function | taurine dioxygenase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006790 | biological_process | sulfur compound metabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019439 | biological_process | obsolete aromatic compound catabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0051213 | molecular_function | dioxygenase activity |
F | 0000908 | molecular_function | taurine dioxygenase activity |
F | 0005737 | cellular_component | cytoplasm |
F | 0006790 | biological_process | sulfur compound metabolic process |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0019439 | biological_process | obsolete aromatic compound catabolic process |
F | 0046872 | molecular_function | metal ion binding |
F | 0051213 | molecular_function | dioxygenase activity |
J | 0000908 | molecular_function | taurine dioxygenase activity |
J | 0005737 | cellular_component | cytoplasm |
J | 0006790 | biological_process | sulfur compound metabolic process |
J | 0016491 | molecular_function | oxidoreductase activity |
J | 0019439 | biological_process | obsolete aromatic compound catabolic process |
J | 0046872 | molecular_function | metal ion binding |
J | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue CO A 301 |
Chain | Residue |
A | HIS111 |
A | ASP113 |
A | HIS270 |
A | AKG303 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue FTJ A 302 |
Chain | Residue |
A | LYS169 |
A | TRP180 |
A | PHE182 |
A | VAL220 |
A | TYR221 |
A | AKG303 |
A | HOH456 |
A | ARG104 |
A | GLY107 |
A | HIS111 |
A | ASP113 |
A | SER114 |
site_id | AC3 |
Number of Residues | 13 |
Details | binding site for residue AKG A 303 |
Chain | Residue |
A | ILE95 |
A | GLY107 |
A | HIS111 |
A | ASP113 |
A | MET126 |
A | THR138 |
A | HIS270 |
A | ALA272 |
A | ARG281 |
A | ARG285 |
A | CO301 |
A | FTJ302 |
A | HOH461 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CL A 304 |
Chain | Residue |
A | ARG72 |
A | PRO76 |
A | VAL77 |
B | ARG72 |
B | PRO76 |
B | VAL77 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue CO B 301 |
Chain | Residue |
B | HIS111 |
B | ASP113 |
B | HIS270 |
B | AKG303 |
site_id | AC6 |
Number of Residues | 14 |
Details | binding site for residue FTJ B 302 |
Chain | Residue |
B | ARG104 |
B | GLY107 |
B | ASP108 |
B | ASP109 |
B | HIS111 |
B | ASP113 |
B | SER114 |
B | LYS169 |
B | TRP180 |
B | PHE182 |
B | VAL220 |
B | TYR221 |
B | HOH408 |
B | HOH481 |
site_id | AC7 |
Number of Residues | 11 |
Details | binding site for residue AKG B 303 |
Chain | Residue |
B | ILE95 |
B | HIS111 |
B | ASP113 |
B | MET126 |
B | THR138 |
B | HIS270 |
B | ALA272 |
B | ARG281 |
B | ARG285 |
B | CO301 |
B | HOH435 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue CO F 301 |
Chain | Residue |
F | HIS111 |
F | ASP113 |
F | HIS270 |
F | AKG303 |
site_id | AC9 |
Number of Residues | 12 |
Details | binding site for residue FTJ F 302 |
Chain | Residue |
F | ILE82 |
F | ARG104 |
F | GLY107 |
F | HIS111 |
F | ASP113 |
F | SER114 |
F | LYS169 |
F | TRP180 |
F | PHE182 |
F | VAL220 |
F | TYR221 |
F | AKG303 |
site_id | AD1 |
Number of Residues | 12 |
Details | binding site for residue AKG F 303 |
Chain | Residue |
F | ILE95 |
F | HIS111 |
F | ASP113 |
F | MET126 |
F | THR138 |
F | HIS270 |
F | ALA272 |
F | ARG281 |
F | ARG285 |
F | CO301 |
F | FTJ302 |
F | HOH420 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue CL F 304 |
Chain | Residue |
F | ARG72 |
F | PRO76 |
F | VAL77 |
J | ARG72 |
J | PRO76 |
J | VAL77 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue CO J 301 |
Chain | Residue |
J | ASP113 |
J | HIS270 |
J | AKG303 |
J | HIS111 |
site_id | AD4 |
Number of Residues | 13 |
Details | binding site for residue FTJ J 302 |
Chain | Residue |
J | ARG104 |
J | GLY107 |
J | ASP108 |
J | HIS111 |
J | ASP113 |
J | SER114 |
J | LYS169 |
J | TRP180 |
J | PHE182 |
J | VAL220 |
J | TYR221 |
J | HOH424 |
J | HOH461 |
site_id | AD5 |
Number of Residues | 12 |
Details | binding site for residue AKG J 303 |
Chain | Residue |
J | ILE95 |
J | GLY107 |
J | HIS111 |
J | ASP113 |
J | MET126 |
J | THR138 |
J | HIS270 |
J | ALA272 |
J | ARG281 |
J | ARG285 |
J | CO301 |
J | HOH445 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P37610 |
Chain | Residue | Details |
A | HIS111 | |
B | TRP255 | |
B | HIS270 | |
B | ARG281 | |
F | HIS111 | |
F | ASP113 | |
F | THR138 | |
F | TRP255 | |
F | HIS270 | |
F | ARG281 | |
J | HIS111 | |
A | ASP113 | |
J | ASP113 | |
J | THR138 | |
J | TRP255 | |
J | HIS270 | |
J | ARG281 | |
A | THR138 | |
A | TRP255 | |
A | HIS270 | |
A | ARG281 | |
B | HIS111 | |
B | ASP113 | |
B | THR138 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | SITE: Contributes to enantiospecificity => ECO:0000303|PubMed:16731970 |
Chain | Residue | Details |
A | TYR221 | |
A | ARG285 | |
B | TYR221 | |
B | ARG285 | |
F | TYR221 | |
F | ARG285 | |
J | TYR221 | |
J | ARG285 |