6PYY
Crystal Structure of human Tryptophan 2,3-dioxygenase in complex with PF-06840003 in Active Site and Exo site
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004833 | molecular_function | L-tryptophan 2,3-dioxygenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006569 | biological_process | L-tryptophan catabolic process |
| A | 0016597 | molecular_function | amino acid binding |
| A | 0019441 | biological_process | obsolete L-tryptophan catabolic process to L-kynurenine |
| A | 0020037 | molecular_function | heme binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045471 | biological_process | response to ethanol |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0051414 | biological_process | response to cortisol |
| A | 0071548 | biological_process | response to dexamethasone |
| A | 1904842 | biological_process | response to nitroglycerin |
| B | 0004833 | molecular_function | L-tryptophan 2,3-dioxygenase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006569 | biological_process | L-tryptophan catabolic process |
| B | 0016597 | molecular_function | amino acid binding |
| B | 0019441 | biological_process | obsolete L-tryptophan catabolic process to L-kynurenine |
| B | 0020037 | molecular_function | heme binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0045471 | biological_process | response to ethanol |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0051414 | biological_process | response to cortisol |
| B | 0071548 | biological_process | response to dexamethasone |
| B | 1904842 | biological_process | response to nitroglycerin |
| C | 0004833 | molecular_function | L-tryptophan 2,3-dioxygenase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006569 | biological_process | L-tryptophan catabolic process |
| C | 0016597 | molecular_function | amino acid binding |
| C | 0019441 | biological_process | obsolete L-tryptophan catabolic process to L-kynurenine |
| C | 0020037 | molecular_function | heme binding |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0045471 | biological_process | response to ethanol |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051289 | biological_process | protein homotetramerization |
| C | 0051414 | biological_process | response to cortisol |
| C | 0071548 | biological_process | response to dexamethasone |
| C | 1904842 | biological_process | response to nitroglycerin |
| D | 0004833 | molecular_function | L-tryptophan 2,3-dioxygenase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006569 | biological_process | L-tryptophan catabolic process |
| D | 0016597 | molecular_function | amino acid binding |
| D | 0019441 | biological_process | obsolete L-tryptophan catabolic process to L-kynurenine |
| D | 0020037 | molecular_function | heme binding |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0045471 | biological_process | response to ethanol |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051289 | biological_process | protein homotetramerization |
| D | 0051414 | biological_process | response to cortisol |
| D | 0071548 | biological_process | response to dexamethasone |
| D | 1904842 | biological_process | response to nitroglycerin |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue HEM A 401 |
| Chain | Residue |
| A | HIS76 |
| A | ARG325 |
| A | HIS328 |
| A | MET331 |
| A | VAL332 |
| A | MET335 |
| A | GLY341 |
| A | GLY343 |
| A | SER345 |
| A | TYR350 |
| A | H7S402 |
| A | TYR79 |
| A | HOH502 |
| A | HOH552 |
| A | PHE140 |
| A | SER151 |
| A | GLY152 |
| A | PHE153 |
| A | PHE158 |
| A | ARG159 |
| A | ASN176 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue H7S A 402 |
| Chain | Residue |
| A | PHE72 |
| A | HIS76 |
| A | ARG144 |
| A | ALA150 |
| A | SER151 |
| A | LEU336 |
| A | THR342 |
| A | HEM401 |
| B | TYR42 |
| B | TYR45 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue H7S A 403 |
| Chain | Residue |
| A | ARG103 |
| A | GLU105 |
| A | TRP208 |
| A | ARG211 |
| A | THR212 |
| A | PRO213 |
| A | ARG303 |
| A | PHE304 |
| A | HOH533 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue HEM B 401 |
| Chain | Residue |
| B | HIS76 |
| B | TYR79 |
| B | LEU132 |
| B | SER151 |
| B | GLY152 |
| B | PHE153 |
| B | PHE158 |
| B | ARG159 |
| B | ARG325 |
| B | HIS328 |
| B | MET331 |
| B | VAL332 |
| B | GLY341 |
| B | THR342 |
| B | GLY343 |
| B | GLY344 |
| B | SER345 |
| B | GLY347 |
| B | TYR350 |
| B | H7S402 |
| B | HOH503 |
| B | HOH538 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue H7S B 402 |
| Chain | Residue |
| A | TYR42 |
| A | TYR45 |
| B | PHE72 |
| B | HIS76 |
| B | ARG144 |
| B | ALA150 |
| B | SER151 |
| B | LEU336 |
| B | THR342 |
| B | HEM401 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue H7S B 403 |
| Chain | Residue |
| B | VAL102 |
| B | ARG103 |
| B | GLU105 |
| B | TRP208 |
| B | ARG211 |
| B | THR212 |
| B | PRO213 |
| B | ARG303 |
| B | PHE304 |
| B | HOH517 |
| B | HOH532 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | binding site for residue HEM C 401 |
| Chain | Residue |
| C | TYR350 |
| C | THR354 |
| C | H7S402 |
| C | HOH501 |
| D | TYR42 |
| C | HIS76 |
| C | MET135 |
| C | SER151 |
| C | GLY152 |
| C | PHE153 |
| C | PHE158 |
| C | ARG159 |
| C | TRP324 |
| C | HIS328 |
| C | MET331 |
| C | VAL332 |
| C | MET335 |
| C | GLY341 |
| C | GLY343 |
| C | SER345 |
| C | GLY347 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue H7S C 402 |
| Chain | Residue |
| C | PHE72 |
| C | HIS76 |
| C | ARG144 |
| C | ALA150 |
| C | SER151 |
| C | LEU336 |
| C | THR342 |
| C | HEM401 |
| D | TYR42 |
| D | TYR45 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue H7S C 403 |
| Chain | Residue |
| C | ARG103 |
| C | GLU105 |
| C | TRP208 |
| C | ARG211 |
| C | THR212 |
| C | PRO213 |
| C | ARG303 |
| C | PHE304 |
| site_id | AD1 |
| Number of Residues | 19 |
| Details | binding site for residue HEM D 401 |
| Chain | Residue |
| C | TYR42 |
| D | PHE72 |
| D | HIS76 |
| D | TYR79 |
| D | SER151 |
| D | GLY152 |
| D | PHE158 |
| D | ARG159 |
| D | TYR175 |
| D | ARG325 |
| D | HIS328 |
| D | MET331 |
| D | VAL332 |
| D | MET335 |
| D | TYR350 |
| D | THR354 |
| D | H7S402 |
| D | HOH534 |
| D | HOH550 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue H7S D 402 |
| Chain | Residue |
| C | TYR42 |
| C | TYR45 |
| D | PHE72 |
| D | HIS76 |
| D | ALA150 |
| D | SER151 |
| D | HEM401 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue H7S D 403 |
| Chain | Residue |
| D | ARG103 |
| D | TRP208 |
| D | ARG211 |
| D | THR212 |
| D | PRO213 |
| D | ARG303 |
| D | PHE304 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 23 |
| 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 |
