2NW7
Crystal Structure of Tryptophan 2,3-dioxygenase (TDO) from Xanthomonas campestris in complex with ferric heme. Northeast Structural Genomics Target XcR13
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004833 | molecular_function | L-tryptophan 2,3-dioxygenase activity |
| A | 0006569 | biological_process | L-tryptophan catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019441 | biological_process | L-tryptophan catabolic process to kynurenine |
| A | 0019442 | biological_process | L-tryptophan catabolic process to acetyl-CoA |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| B | 0004833 | molecular_function | L-tryptophan 2,3-dioxygenase activity |
| B | 0006569 | biological_process | L-tryptophan catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019441 | biological_process | L-tryptophan catabolic process to kynurenine |
| B | 0019442 | biological_process | L-tryptophan catabolic process to acetyl-CoA |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051213 | molecular_function | dioxygenase activity |
| C | 0004833 | molecular_function | L-tryptophan 2,3-dioxygenase activity |
| C | 0006569 | biological_process | L-tryptophan catabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019441 | biological_process | L-tryptophan catabolic process to kynurenine |
| C | 0019442 | biological_process | L-tryptophan catabolic process to acetyl-CoA |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051213 | molecular_function | dioxygenase activity |
| D | 0004833 | molecular_function | L-tryptophan 2,3-dioxygenase activity |
| D | 0006569 | biological_process | L-tryptophan catabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019441 | biological_process | L-tryptophan catabolic process to kynurenine |
| D | 0019442 | biological_process | L-tryptophan catabolic process to acetyl-CoA |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM A 401 |
| Chain | Residue |
| A | PHE51 |
| A | HIS240 |
| A | VAL244 |
| A | PHE262 |
| A | HIS55 |
| A | TRP102 |
| A | LEU105 |
| A | SER124 |
| A | GLY125 |
| A | TYR131 |
| A | ARG132 |
| A | TRP236 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM B 401 |
| Chain | Residue |
| B | PHE51 |
| B | HIS55 |
| B | TRP102 |
| B | LEU105 |
| B | SER124 |
| B | GLY125 |
| B | PHE126 |
| B | TYR131 |
| B | HIS240 |
| B | VAL244 |
| B | GLY259 |
| B | PHE262 |
| B | LEU263 |
| C | TYR24 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM C 401 |
| Chain | Residue |
| C | PHE51 |
| C | HIS55 |
| C | LEU105 |
| C | SER124 |
| C | GLY125 |
| C | PHE126 |
| C | TYR131 |
| C | ARG132 |
| C | HIS240 |
| C | VAL244 |
| C | ILE248 |
| C | PHE262 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HEM D 401 |
| Chain | Residue |
| D | PHE51 |
| D | HIS55 |
| D | LEU105 |
| D | SER124 |
| D | GLY125 |
| D | PHE126 |
| D | TYR131 |
| D | HIS240 |
| D | VAL244 |
| D | PHE262 |
| D | LEU263 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01972","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17197414","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18783250","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2NW8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BK9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01972","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17197414","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18783250","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2NW8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BK9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3E08","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01972","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17197414","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18783250","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2NW7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NW8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NW9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BK9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3E08","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
