8QV7
Crystal structure of human TDO with alpha-methyl-L-tryptophan
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004833 | molecular_function | L-tryptophan 2,3-dioxygenase activity |
| A | 0019441 | biological_process | L-tryptophan catabolic process to 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 | L-tryptophan catabolic process to 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 | L-tryptophan catabolic process to 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 | L-tryptophan catabolic process to kynurenine |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03020","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27762317","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5TI9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_03020","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27762317","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5TI9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
