2NW9
Crystal Structure of Tryptophan 2,3-dioxygenase (TDO) from Xanthomonas campestris in complex with ferrous heme and 6-fluoro-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 | tryptophan catabolic process |
A | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
A | 0019442 | biological_process | 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 | tryptophan catabolic process |
B | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
B | 0019442 | biological_process | 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 | GLU207 |
B | HOH498 |
B | HOH510 |
B | HOH681 |
B | HOH693 |
B | HOH721 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 308 |
Chain | Residue |
B | HOH687 |
B | HOH703 |
B | HOH479 |
B | HOH618 |
B | HOH626 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE FT6 A 307 |
Chain | Residue |
A | PHE51 |
A | HIS55 |
A | TYR113 |
A | ARG117 |
A | LEU120 |
A | SER123 |
A | GLY253 |
A | THR254 |
A | HEM401 |
A | HOH426 |
B | TYR24 |
B | TYR27 |
B | LEU28 |
site_id | AC4 |
Number of Residues | 26 |
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 | GLY253 |
A | THR254 |
A | GLY255 |
A | GLY256 |
A | SER257 |
A | GLY259 |
A | FT6307 |
A | HOH415 |
A | HOH426 |
A | HOH459 |
A | HOH517 |
A | HOH551 |
B | TYR24 |
site_id | AC5 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM B 401 |
Chain | Residue |
A | TYR24 |
A | ARG215 |
B | PHE51 |
B | GLN54 |
B | HIS55 |
B | SER58 |
B | TRP102 |
B | SER124 |
B | GLY125 |
B | PHE126 |
B | TYR131 |
B | ARG132 |
B | HIS240 |
B | VAL244 |
B | VAL247 |
B | ILE248 |
B | SER258 |
B | GLY259 |
B | PHE262 |
B | HOH419 |
B | HOH449 |
B | HOH463 |
B | HOH701 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01972, ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250, ECO:0007744|PDB:2NW8, ECO:0007744|PDB:3BK9 |
Chain | Residue | Details |
A | PHE51 | |
B | PHE51 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01972, ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250, ECO:0007744|PDB:2NW8, ECO:0007744|PDB:3BK9, ECO:0007744|PDB:3E08 |
Chain | Residue | Details |
A | TYR113 | |
A | ARG117 | |
A | THR254 | |
B | TYR113 | |
B | ARG117 | |
B | THR254 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_01972, ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250, ECO:0007744|PDB:2NW7, ECO:0007744|PDB:2NW8, ECO:0007744|PDB:2NW9, ECO:0007744|PDB:3BK9, ECO:0007744|PDB:3E08 |
Chain | Residue | Details |
A | HIS240 | |
B | HIS240 |