1GQW
Taurine/alpha-ketoglutarate Dioxygenase from Escherichia coli
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 | 0008198 | molecular_function | ferrous iron binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
A | 0019529 | biological_process | taurine catabolic process |
A | 0031418 | molecular_function | L-ascorbic acid binding |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0051213 | molecular_function | dioxygenase activity |
A | 0051289 | biological_process | protein homotetramerization |
A | 1990205 | cellular_component | taurine dioxygenase complex |
B | 0000908 | molecular_function | taurine dioxygenase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006790 | biological_process | sulfur compound metabolic process |
B | 0008198 | molecular_function | ferrous iron binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
B | 0019529 | biological_process | taurine catabolic process |
B | 0031418 | molecular_function | L-ascorbic acid binding |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0051213 | molecular_function | dioxygenase activity |
B | 0051289 | biological_process | protein homotetramerization |
B | 1990205 | cellular_component | taurine dioxygenase complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE2 A 301 |
Chain | Residue |
A | HIS99 |
A | ASP101 |
A | HIS255 |
A | AKG352 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE2 B 301 |
Chain | Residue |
B | HIS99 |
B | ASP101 |
B | HIS255 |
B | AKG352 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TAU A 351 |
Chain | Residue |
A | TYR73 |
A | ASN95 |
A | HIS99 |
A | ASP101 |
A | VAL102 |
A | SER158 |
A | PHE159 |
A | PHE206 |
A | ARG270 |
A | HIS70 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE AKG A 352 |
Chain | Residue |
A | LEU85 |
A | ASN95 |
A | HIS99 |
A | ASP101 |
A | LEU114 |
A | THR126 |
A | TRP240 |
A | HIS255 |
A | ARG266 |
A | MET268 |
A | ARG270 |
A | FE2301 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TAU B 351 |
Chain | Residue |
B | HIS70 |
B | TYR73 |
B | ASN95 |
B | ASP101 |
B | VAL102 |
B | PHE104 |
B | SER158 |
B | PHE159 |
B | PHE206 |
B | ARG270 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE AKG B 352 |
Chain | Residue |
B | LEU85 |
B | ASN95 |
B | HIS99 |
B | ASP101 |
B | LEU114 |
B | THR126 |
B | TRP240 |
B | HIS255 |
B | ARG266 |
B | MET268 |
B | ARG270 |
B | FE2301 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11955067, ECO:0000269|PubMed:12741810 |
Chain | Residue | Details |
A | HIS70 | |
A | ARG270 | |
B | HIS70 | |
B | TYR73 | |
B | ASN95 | |
B | HIS99 | |
B | ASP101 | |
B | VAL102 | |
B | THR126 | |
B | HIS255 | |
B | ARG266 | |
A | TYR73 | |
B | ARG270 | |
A | ASN95 | |
A | HIS99 | |
A | ASP101 | |
A | VAL102 | |
A | THR126 | |
A | HIS255 | |
A | ARG266 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | MOD_RES: 3-hydroxytryptophan; by autocatalysis => ECO:0000269|PubMed:11955067 |
Chain | Residue | Details |
A | TRP128 | |
A | TRP240 | |
A | TRP248 | |
B | TRP128 | |
B | TRP240 | |
B | TRP248 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 129 |
Chain | Residue | Details |
A | HIS99 | metal ligand |
A | ASP101 | metal ligand |
A | HIS255 | metal ligand |
A | ARG270 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 129 |
Chain | Residue | Details |
B | HIS99 | metal ligand |
B | ASP101 | metal ligand |
B | HIS255 | metal ligand |
B | ARG270 | electrostatic stabiliser, hydrogen bond donor |