1YW0
Crystal structure of the tryptophan 2,3-dioxygenase from Xanthomonas campestris. 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 | 0019441 | biological_process | obsolete L-tryptophan catabolic process to L-kynurenine |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004833 | molecular_function | L-tryptophan 2,3-dioxygenase activity |
| B | 0019441 | biological_process | obsolete L-tryptophan catabolic process to L-kynurenine |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004833 | molecular_function | L-tryptophan 2,3-dioxygenase activity |
| C | 0019441 | biological_process | obsolete L-tryptophan catabolic process to L-kynurenine |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004833 | molecular_function | L-tryptophan 2,3-dioxygenase activity |
| D | 0019441 | biological_process | obsolete L-tryptophan catabolic process to L-kynurenine |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 400 |
| Chain | Residue |
| B | TYR27 |
| B | LEU28 |
| C | ALA36 |
| C | GLN37 |
| C | GLN38 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | ALA36 |
| A | GLN37 |
| A | GLN38 |
| D | TYR27 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 402 |
| Chain | Residue |
| A | TYR27 |
| D | GLN38 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 403 |
| Chain | Residue |
| B | ALA36 |
| B | GLN37 |
| B | GLN38 |
| C | TYR27 |
| C | ARG29 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 404 |
| Chain | Residue |
| B | LEU108 |
| B | ARG246 |
| D | GLU224 |
| D | ARG279 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 405 |
| Chain | Residue |
| B | GLN38 |
| B | LEU40 |
| C | TYR27 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 406 |
| Chain | Residue |
| A | PHE126 |
| A | GLN127 |
| A | SER128 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 407 |
| Chain | Residue |
| C | LEU34 |
| C | SER35 |
| C | ALA36 |
| C | GLN37 |
| C | GLN38 |
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 |
