2NW8
Crystal Structure of Tryptophan 2,3-dioxygenase (TDO) from Xanthomonas campestris in complex with ferrous heme and tryptophan. Northeast Structural Genomics Target XcR13.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004833 | molecular_function | 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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 307 |
| Chain | Residue |
| B | HOH491 |
| B | HOH497 |
| B | HOH500 |
| B | HOH574 |
| B | HOH744 |
| B | HOH752 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 308 |
| Chain | Residue |
| B | HOH564 |
| B | HOH596 |
| B | HOH764 |
| B | GLU207 |
| B | HOH524 |
| B | HOH551 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TRP A 307 |
| Chain | Residue |
| A | PHE51 |
| A | HIS55 |
| A | TYR113 |
| A | ARG117 |
| A | SER123 |
| A | GLY253 |
| A | THR254 |
| A | HEM401 |
| A | HOH402 |
| B | TYR24 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE TRP A 308 |
| Chain | Residue |
| A | ARG85 |
| A | LYS92 |
| A | TYR220 |
| A | SER221 |
| A | GLU224 |
| A | ASP228 |
| A | HOH411 |
| A | HOH422 |
| A | HOH442 |
| A | HOH502 |
| A | HOH698 |
| B | LYS86 |
| B | ALA89 |
| B | HOH536 |
| B | HOH597 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TRP B 309 |
| Chain | Residue |
| A | TYR24 |
| A | ARG215 |
| B | PHE51 |
| B | HIS55 |
| B | TYR113 |
| B | GLY121 |
| B | PRO122 |
| B | SER123 |
| B | HOH402 |
| B | HOH687 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE TRP B 310 |
| Chain | Residue |
| A | LYS86 |
| A | ALA89 |
| A | HOH495 |
| A | HOH539 |
| B | ARG85 |
| B | LYS92 |
| B | TYR220 |
| B | SER221 |
| B | GLU224 |
| B | ASP225 |
| B | ASP228 |
| B | HOH411 |
| B | HOH434 |
| B | HOH517 |
| B | HOH560 |
| site_id | AC7 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE HEM A 401 |
| Chain | Residue |
| A | PHE51 |
| A | GLN54 |
| A | HIS55 |
| A | SER58 |
| A | TRP102 |
| A | LEU105 |
| A | SER124 |
| A | GLY125 |
| A | PHE126 |
| A | TYR131 |
| A | ARG132 |
| A | HIS240 |
| A | VAL244 |
| A | ILE248 |
| A | GLY253 |
| A | THR254 |
| A | GLY255 |
| A | GLY256 |
| A | SER257 |
| A | GLY259 |
| A | TRP307 |
| A | HOH402 |
| A | HOH459 |
| A | HOH514 |
| A | HOH534 |
| A | HOH694 |
| B | TYR24 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM B 401 |
| Chain | Residue |
| B | TYR131 |
| B | ARG132 |
| B | HIS240 |
| B | VAL244 |
| B | ILE248 |
| B | GLY259 |
| B | HOH402 |
| B | HOH489 |
| B | HOH499 |
| B | HOH741 |
| B | HOH751 |
| A | TYR24 |
| A | ARG215 |
| B | PHE51 |
| B | GLN54 |
| B | HIS55 |
| B | SER58 |
| B | TRP102 |
| B | SER124 |
| B | GLY125 |
| B | PHE126 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| 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 | 2 |
| 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 |
