6UD5
Crystal structure of human tryptophan 2,3-dioxygenase in complex with carbon monoxide and tryptophan
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 | 23 |
| Details | binding site for residue HEM A 500 |
| Chain | Residue |
| A | HIS76 |
| A | MET331 |
| A | VAL332 |
| A | MET335 |
| A | GLY341 |
| A | GLY343 |
| A | GLY344 |
| A | SER345 |
| A | TYR350 |
| A | CMO501 |
| A | TRP502 |
| A | TYR79 |
| A | HOH601 |
| A | HOH641 |
| A | HOH691 |
| B | TYR42 |
| A | SER151 |
| A | GLY152 |
| A | PHE153 |
| A | PHE158 |
| A | ARG159 |
| A | ARG325 |
| A | HIS328 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CMO A 501 |
| Chain | Residue |
| A | GLY152 |
| A | HEM500 |
| A | TRP502 |
| A | HOH691 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue TRP A 502 |
| Chain | Residue |
| A | PHE72 |
| A | HIS76 |
| A | PHE140 |
| A | ARG144 |
| A | ALA150 |
| A | LEU336 |
| A | GLY341 |
| A | THR342 |
| A | HEM500 |
| A | CMO501 |
| A | HOH691 |
| B | TYR42 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue TRP A 503 |
| Chain | Residue |
| A | ARG103 |
| A | GLU105 |
| A | TRP208 |
| A | ARG211 |
| A | THR212 |
| A | PRO213 |
| A | ARG303 |
| A | PHE304 |
| A | PRO307 |
| A | HOH622 |
| A | HOH625 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | binding site for residue HEM B 500 |
| Chain | Residue |
| B | HIS76 |
| B | TYR79 |
| B | LEU132 |
| B | SER151 |
| B | GLY152 |
| B | PHE153 |
| B | PHE158 |
| B | ARG159 |
| B | TRP324 |
| B | HIS328 |
| B | MET331 |
| B | VAL332 |
| B | MET335 |
| B | GLY341 |
| B | THR342 |
| B | GLY343 |
| B | GLY344 |
| B | SER345 |
| B | TYR350 |
| B | CMO501 |
| B | TRP502 |
| B | HOH602 |
| B | HOH637 |
| B | HOH685 |
| B | HOH694 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CMO B 501 |
| Chain | Residue |
| B | GLY152 |
| B | HEM500 |
| B | TRP502 |
| B | HOH637 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue TRP B 502 |
| Chain | Residue |
| A | TYR42 |
| A | TYR45 |
| B | PHE72 |
| B | HIS76 |
| B | PHE140 |
| B | ARG144 |
| B | ALA150 |
| B | LEU336 |
| B | GLY341 |
| B | THR342 |
| B | HEM500 |
| B | CMO501 |
| B | HOH637 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue TRP B 503 |
| Chain | Residue |
| B | PHE304 |
| B | PRO307 |
| B | HOH641 |
| B | HOH646 |
| B | ARG103 |
| B | GLU105 |
| B | TRP208 |
| B | ARG211 |
| B | THR212 |
| B | PRO213 |
| B | ARG303 |
| site_id | AC9 |
| Number of Residues | 24 |
| Details | binding site for residue HEM C 500 |
| Chain | Residue |
| C | HIS76 |
| C | TYR79 |
| C | SER151 |
| C | GLY152 |
| C | PHE153 |
| C | PHE158 |
| C | ARG159 |
| C | TRP324 |
| C | ARG325 |
| C | HIS328 |
| C | MET331 |
| C | VAL332 |
| C | MET335 |
| C | GLY341 |
| C | THR342 |
| C | GLY343 |
| C | SER345 |
| C | TYR350 |
| C | CMO501 |
| C | TRP502 |
| C | HOH620 |
| C | HOH647 |
| C | HOH688 |
| D | TYR42 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue CMO C 501 |
| Chain | Residue |
| C | GLY152 |
| C | HEM500 |
| C | TRP502 |
| C | HOH620 |
| site_id | AD2 |
| Number of Residues | 12 |
| Details | binding site for residue TRP C 502 |
| Chain | Residue |
| C | PHE72 |
| C | HIS76 |
| C | PHE140 |
| C | ARG144 |
| C | ALA150 |
| C | LEU336 |
| C | GLY341 |
| C | THR342 |
| C | HEM500 |
| C | CMO501 |
| C | HOH620 |
| D | TYR42 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue TRP C 503 |
| Chain | Residue |
| C | ARG103 |
| C | GLU105 |
| C | TRP208 |
| C | ARG211 |
| C | THR212 |
| C | PRO213 |
| C | ARG303 |
| C | PHE304 |
| C | PRO307 |
| C | HOH601 |
| site_id | AD4 |
| Number of Residues | 24 |
| Details | binding site for residue HEM D 500 |
| Chain | Residue |
| D | HIS76 |
| D | TYR79 |
| D | SER151 |
| D | GLY152 |
| D | PHE153 |
| D | PHE158 |
| D | ARG159 |
| D | ARG325 |
| D | HIS328 |
| D | MET331 |
| D | VAL332 |
| D | MET335 |
| D | GLY341 |
| D | THR342 |
| D | GLY343 |
| D | GLY344 |
| D | SER345 |
| D | TYR350 |
| D | THR354 |
| D | CMO501 |
| D | TRP502 |
| D | HOH650 |
| D | HOH688 |
| D | HOH706 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue CMO D 501 |
| Chain | Residue |
| D | GLY152 |
| D | HEM500 |
| D | TRP502 |
| D | HOH650 |
| site_id | AD6 |
| Number of Residues | 12 |
| Details | binding site for residue TRP D 502 |
| Chain | Residue |
| C | TYR42 |
| D | PHE72 |
| D | HIS76 |
| D | PHE140 |
| D | ARG144 |
| D | ALA150 |
| D | LEU336 |
| D | GLY341 |
| D | THR342 |
| D | HEM500 |
| D | CMO501 |
| D | HOH650 |
| site_id | AD7 |
| Number of Residues | 10 |
| Details | binding site for residue TRP D 503 |
| Chain | Residue |
| D | ARG103 |
| D | GLU105 |
| D | TRP208 |
| D | ARG211 |
| D | PRO213 |
| D | ARG303 |
| D | PHE304 |
| D | PRO307 |
| D | HOH633 |
| D | HOH701 |
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 |
| B | ARG144 | |
| B | THR342 | |
| C | PHE72 | |
| C | ARG144 | |
| C | THR342 | |
| D | PHE72 | |
| D | ARG144 | |
| D | THR342 | |
| A | ARG144 | |
| A | THR342 | |
| B | PHE72 | |
| A | PHE72 |
| 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 |
| C | HIS328 | |
| D | HIS328 | |
| A | HIS328 | |
| B | HIS328 |
