6EDH
Taurine:2OG dioxygenase (TauD) bound to the vanadyl ion, taurine, and succinate
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 | 3 |
| Details | binding site for residue ACT A 301 |
| Chain | Residue |
| A | LEU114 |
| A | THR126 |
| A | ARG266 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue VVO A 302 |
| Chain | Residue |
| A | ASN95 |
| A | HIS99 |
| A | ASP101 |
| A | HIS255 |
| A | HOH436 |
| A | HOH485 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue SIN B 301 |
| Chain | Residue |
| B | LEU85 |
| B | ASN95 |
| B | HIS99 |
| B | ASP101 |
| B | LEU114 |
| B | THR126 |
| B | HIS255 |
| B | ALA257 |
| B | ARG266 |
| B | ARG270 |
| B | VVO302 |
| B | HOH507 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue VVO B 302 |
| Chain | Residue |
| B | ASN95 |
| B | HIS99 |
| B | ASP101 |
| B | HIS255 |
| B | ARG270 |
| B | SIN301 |
| B | TAU303 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue TAU B 303 |
| Chain | Residue |
| B | HIS70 |
| B | TYR73 |
| B | ASN95 |
| B | ASP101 |
| B | VAL102 |
| B | PHE159 |
| B | PHE206 |
| B | ARG270 |
| B | VVO302 |
| B | HOH402 |
| B | HOH423 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue 1PE B 304 |
| Chain | Residue |
| B | ALA137 |
| B | ARG143 |
| B | ALA282 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue PEG B 305 |
| Chain | Residue |
| B | TYR135 |
| B | GLN144 |
| B | HOH406 |
| B | HOH406 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue PG4 B 306 |
| Chain | Residue |
| A | ASP276 |
| B | HIS70 |
| B | VAL72 |
| B | TYR73 |
| B | HIS75 |
| B | ASP80 |
| B | ARG173 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11955067","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12741810","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"3-hydroxytryptophan; by autocatalysis","evidences":[{"source":"PubMed","id":"11955067","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 |
