1OS7
Crystal structure of TauD with iron, alpha-ketoglutarate and Taurine bound at pH 7.5
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 |
| C | 0000908 | molecular_function | taurine dioxygenase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006790 | biological_process | sulfur compound metabolic process |
| C | 0008198 | molecular_function | ferrous iron binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| C | 0019529 | biological_process | taurine catabolic process |
| C | 0031418 | molecular_function | L-ascorbic acid binding |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051213 | molecular_function | dioxygenase activity |
| C | 0051289 | biological_process | protein homotetramerization |
| C | 1990205 | cellular_component | taurine dioxygenase complex |
| D | 0000908 | molecular_function | taurine dioxygenase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006790 | biological_process | sulfur compound metabolic process |
| D | 0008198 | molecular_function | ferrous iron binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| D | 0019529 | biological_process | taurine catabolic process |
| D | 0031418 | molecular_function | L-ascorbic acid binding |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051213 | molecular_function | dioxygenase activity |
| D | 0051289 | biological_process | protein homotetramerization |
| D | 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 302 |
| Chain | Residue |
| A | HIS99 |
| A | ASP101 |
| A | HIS255 |
| A | AKG501 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE2 B 302 |
| Chain | Residue |
| B | HIS99 |
| B | ASP101 |
| B | HIS255 |
| B | AKG502 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE2 C 302 |
| Chain | Residue |
| C | ASP101 |
| C | HIS255 |
| C | AKG503 |
| C | HIS99 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE2 D 302 |
| Chain | Residue |
| D | HIS99 |
| D | ASP101 |
| D | HIS255 |
| D | AKG504 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TAU A 401 |
| Chain | Residue |
| A | HIS70 |
| A | ASN95 |
| A | ASP101 |
| A | VAL102 |
| A | PHE159 |
| A | PHE206 |
| A | ARG270 |
| A | HOH540 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AKG A 501 |
| 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 | FE2302 |
| A | HOH546 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TAU B 402 |
| Chain | Residue |
| B | HIS70 |
| B | TYR73 |
| B | ASP94 |
| B | ASN95 |
| B | HIS99 |
| B | VAL102 |
| B | PHE159 |
| B | PHE206 |
| B | ARG270 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AKG B 502 |
| Chain | Residue |
| B | ASN95 |
| B | HIS99 |
| B | ASP101 |
| B | LEU114 |
| B | THR126 |
| B | TRP240 |
| B | HIS255 |
| B | ARG266 |
| B | ARG270 |
| B | FE2302 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TAU C 403 |
| Chain | Residue |
| C | HIS70 |
| C | TYR73 |
| C | ASN95 |
| C | HIS99 |
| C | ASP101 |
| C | VAL102 |
| C | PHE104 |
| C | PHE159 |
| C | PHE206 |
| C | ARG270 |
| C | HOH565 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AKG C 503 |
| Chain | Residue |
| C | LEU85 |
| C | ASN95 |
| C | HIS99 |
| C | ASP101 |
| C | LEU114 |
| C | THR126 |
| C | TRP240 |
| C | HIS255 |
| C | ALA257 |
| C | ARG266 |
| C | ARG270 |
| C | FE2302 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AKG D 504 |
| Chain | Residue |
| D | ASN95 |
| D | HIS99 |
| D | ASP101 |
| D | LEU114 |
| D | THR126 |
| D | HIS255 |
| D | ARG266 |
| D | ARG270 |
| D | FE2302 |
| D | HOH602 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| 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 | 12 |
| 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 | CSA1 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 15924433, 15023059 |
| Chain | Residue | Details |
| A | ARG270 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 15924433, 15023059 |
| Chain | Residue | Details |
| B | ARG270 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 15924433, 15023059 |
| Chain | Residue | Details |
| C | ARG270 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 15924433, 15023059 |
| Chain | Residue | Details |
| D | ARG270 |
| 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 |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 129 |
| Chain | Residue | Details |
| C | HIS99 | metal ligand |
| C | ASP101 | metal ligand |
| C | HIS255 | metal ligand |
| C | ARG270 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 129 |
| Chain | Residue | Details |
| D | HIS99 | metal ligand |
| D | ASP101 | metal ligand |
| D | HIS255 | metal ligand |
| D | ARG270 | electrostatic stabiliser, hydrogen bond donor |
