6D3H
FT_T dioxygenase with bound dichlorprop
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 |
I | 0000908 | molecular_function | taurine dioxygenase activity |
I | 0005737 | cellular_component | cytoplasm |
I | 0006790 | biological_process | sulfur compound metabolic process |
I | 0016491 | molecular_function | oxidoreductase activity |
I | 0019439 | biological_process | obsolete aromatic compound catabolic process |
I | 0046872 | molecular_function | metal ion binding |
I | 0051213 | molecular_function | dioxygenase activity |
M | 0000908 | molecular_function | taurine dioxygenase activity |
M | 0005737 | cellular_component | cytoplasm |
M | 0006790 | biological_process | sulfur compound metabolic process |
M | 0016491 | molecular_function | oxidoreductase activity |
M | 0019439 | biological_process | obsolete aromatic compound catabolic process |
M | 0046872 | molecular_function | metal ion binding |
M | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue FTV A 301 |
Chain | Residue |
A | VAL80 |
A | LEU83 |
A | GLY107 |
A | HIS111 |
A | ASP113 |
A | SER114 |
A | PHE182 |
A | TYR221 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue CO A 302 |
Chain | Residue |
A | ASP113 |
A | HIS270 |
A | AKG303 |
A | HIS111 |
site_id | AC3 |
Number of Residues | 11 |
Details | binding site for residue AKG A 303 |
Chain | Residue |
A | ILE95 |
A | HIS111 |
A | ASP113 |
A | MET126 |
A | THR138 |
A | HIS270 |
A | ALA272 |
A | ARG281 |
A | ARG285 |
A | CO302 |
A | HOH439 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue CL A 304 |
Chain | Residue |
A | THR63 |
B | THR63 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue FTV B 301 |
Chain | Residue |
B | ILE82 |
B | GLY107 |
B | HIS111 |
B | ASP113 |
B | SER114 |
B | TYR221 |
B | AKG303 |
B | HOH476 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue CO B 302 |
Chain | Residue |
B | HIS111 |
B | ASP113 |
B | HIS270 |
B | AKG303 |
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 | ARG281 |
B | ARG285 |
B | FTV301 |
B | CO302 |
B | HOH419 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue CL B 304 |
Chain | Residue |
A | ARG72 |
A | VAL77 |
B | ARG72 |
B | PRO76 |
B | VAL77 |
site_id | AC9 |
Number of Residues | 9 |
Details | binding site for residue FTV I 301 |
Chain | Residue |
I | ILE82 |
I | ARG104 |
I | GLY107 |
I | HIS111 |
I | ASP113 |
I | SER114 |
I | TYR221 |
I | AKG303 |
I | HOH459 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue CO I 302 |
Chain | Residue |
I | HIS111 |
I | ASP113 |
I | HIS270 |
I | AKG303 |
site_id | AD2 |
Number of Residues | 11 |
Details | binding site for residue AKG I 303 |
Chain | Residue |
I | ILE95 |
I | HIS111 |
I | ASP113 |
I | MET126 |
I | THR138 |
I | HIS270 |
I | ARG281 |
I | ARG285 |
I | FTV301 |
I | CO302 |
I | HOH429 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue CL I 304 |
Chain | Residue |
I | THR63 |
M | THR63 |
M | GLU65 |
site_id | AD4 |
Number of Residues | 9 |
Details | binding site for residue FTV M 301 |
Chain | Residue |
M | VAL80 |
M | LEU83 |
M | ARG104 |
M | GLY107 |
M | HIS111 |
M | ASP113 |
M | SER114 |
M | TYR221 |
M | AKG303 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue CO M 302 |
Chain | Residue |
M | HIS111 |
M | ASP113 |
M | HIS270 |
M | AKG303 |
site_id | AD6 |
Number of Residues | 12 |
Details | binding site for residue AKG M 303 |
Chain | Residue |
M | ALA272 |
M | ARG281 |
M | ARG285 |
M | FTV301 |
M | CO302 |
M | HOH434 |
M | ILE95 |
M | HIS111 |
M | ASP113 |
M | MET126 |
M | THR138 |
M | HIS270 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue CL M 304 |
Chain | Residue |
I | ARG72 |
I | PRO76 |
I | VAL77 |
M | ARG72 |
M | PRO76 |
M | VAL77 |
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 | |
I | HIS111 | |
I | ASP113 | |
I | THR138 | |
I | TRP255 | |
I | HIS270 | |
I | ARG281 | |
M | HIS111 | |
A | ASP113 | |
M | ASP113 | |
M | THR138 | |
M | TRP255 | |
M | HIS270 | |
M | 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 | |
I | TYR221 | |
I | ARG285 | |
M | TYR221 | |
M | ARG285 |