6A4I
Crystal Structure of human TDO inhibitor complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004833 | molecular_function | tryptophan 2,3-dioxygenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006568 | biological_process | tryptophan metabolic process |
| A | 0006569 | biological_process | tryptophan catabolic process |
| A | 0016597 | molecular_function | amino acid binding |
| A | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
| A | 0019442 | biological_process | tryptophan catabolic process to acetyl-CoA |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme 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 | 1904842 | biological_process | response to nitroglycerin |
| B | 0004833 | molecular_function | tryptophan 2,3-dioxygenase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006568 | biological_process | tryptophan metabolic process |
| B | 0006569 | biological_process | tryptophan catabolic process |
| B | 0016597 | molecular_function | amino acid binding |
| B | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
| B | 0019442 | biological_process | tryptophan catabolic process to acetyl-CoA |
| B | 0019825 | molecular_function | oxygen binding |
| B | 0020037 | molecular_function | heme 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 | 1904842 | biological_process | response to nitroglycerin |
| C | 0004833 | molecular_function | tryptophan 2,3-dioxygenase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006568 | biological_process | tryptophan metabolic process |
| C | 0006569 | biological_process | tryptophan catabolic process |
| C | 0016597 | molecular_function | amino acid binding |
| C | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
| C | 0019442 | biological_process | tryptophan catabolic process to acetyl-CoA |
| C | 0019825 | molecular_function | oxygen binding |
| C | 0020037 | molecular_function | heme 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 | 1904842 | biological_process | response to nitroglycerin |
| D | 0004833 | molecular_function | tryptophan 2,3-dioxygenase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006568 | biological_process | tryptophan metabolic process |
| D | 0006569 | biological_process | tryptophan catabolic process |
| D | 0016597 | molecular_function | amino acid binding |
| D | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
| D | 0019442 | biological_process | tryptophan catabolic process to acetyl-CoA |
| D | 0019825 | molecular_function | oxygen binding |
| D | 0020037 | molecular_function | heme 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 | 1904842 | biological_process | response to nitroglycerin |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue HEM A 401 |
| Chain | Residue |
| A | PHE72 |
| A | ARG159 |
| A | TRP324 |
| A | HIS328 |
| A | MET331 |
| A | VAL332 |
| A | MET335 |
| A | TYR350 |
| A | LEU351 |
| A | 9R9402 |
| B | TYR42 |
| A | HIS76 |
| A | LEU132 |
| A | MET135 |
| A | PHE140 |
| A | SER151 |
| A | GLY152 |
| A | PHE153 |
| A | PHE158 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue 9R9 A 402 |
| Chain | Residue |
| A | HIS76 |
| A | ALA150 |
| A | HEM401 |
| B | TYR42 |
| B | TYR45 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue TRP A 403 |
| Chain | Residue |
| A | VAL102 |
| A | ARG103 |
| A | GLU105 |
| A | TRP208 |
| A | ARG211 |
| A | THR212 |
| A | PRO213 |
| A | ARG303 |
| A | PHE304 |
| A | PRO307 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CIT A 404 |
| Chain | Residue |
| A | LYS110 |
| A | ARG114 |
| B | LYS65 |
| B | HIS67 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | binding site for residue HEM B 401 |
| Chain | Residue |
| A | TYR42 |
| B | PHE72 |
| B | HIS76 |
| B | TYR79 |
| B | LEU132 |
| B | SER151 |
| B | GLY152 |
| B | PHE153 |
| B | PHE158 |
| B | ARG159 |
| B | TRP324 |
| B | HIS328 |
| B | VAL332 |
| B | TYR350 |
| B | 9R9402 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue 9R9 B 402 |
| Chain | Residue |
| A | TYR42 |
| A | TYR45 |
| B | HIS76 |
| B | LEU147 |
| B | ALA150 |
| B | HEM401 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue TRP B 403 |
| Chain | Residue |
| B | VAL102 |
| B | ARG103 |
| B | GLU105 |
| B | TRP208 |
| B | ARG211 |
| B | THR212 |
| B | PRO213 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | binding site for residue HEM C 401 |
| Chain | Residue |
| C | PHE72 |
| C | HIS76 |
| C | TYR79 |
| C | LEU132 |
| C | MET135 |
| C | PHE140 |
| C | SER151 |
| C | GLY152 |
| C | PHE153 |
| C | ARG159 |
| C | TYR175 |
| C | HIS328 |
| C | MET331 |
| C | VAL332 |
| C | TYR350 |
| C | LEU351 |
| C | 9R9402 |
| D | TYR42 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue 9R9 C 402 |
| Chain | Residue |
| C | HIS76 |
| C | LEU147 |
| C | ALA150 |
| C | SER151 |
| C | HEM401 |
| D | TYR42 |
| D | TYR45 |
| site_id | AD1 |
| Number of Residues | 12 |
| Details | binding site for residue HEM D 401 |
| Chain | Residue |
| D | VAL332 |
| D | MET335 |
| D | LEU351 |
| D | 9R9402 |
| C | TYR42 |
| D | HIS76 |
| D | PHE140 |
| D | SER151 |
| D | GLY152 |
| D | PHE153 |
| D | PHE158 |
| D | HIS328 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue 9R9 D 402 |
| Chain | Residue |
| C | TYR42 |
| C | TYR45 |
| D | PHE72 |
| D | HIS76 |
| D | LEU147 |
| D | ALA150 |
| D | HEM401 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for residue TRP D 403 |
| Chain | Residue |
| D | ARG103 |
| D | GLU105 |
| D | TRP208 |
| D | ARG211 |
| D | THR212 |
| D | PRO213 |
| D | ILE295 |
| D | ARG303 |
| D | PHE304 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03020, ECO:0000269|PubMed:27762317, ECO:0007744|PDB:5TI9 |
| Chain | Residue | Details |
| A | PHE72 | |
| D | PHE72 | |
| D | ARG144 | |
| D | THR342 | |
| A | ARG144 | |
| A | THR342 | |
| B | PHE72 | |
| B | ARG144 | |
| B | THR342 | |
| C | PHE72 | |
| C | ARG144 | |
| C | THR342 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_03020, ECO:0000269|PubMed:27762317, ECO:0007744|PDB:5TI9 |
| Chain | Residue | Details |
| A | HIS328 | |
| B | HIS328 | |
| C | HIS328 | |
| D | HIS328 |
