2NW8
Crystal Structure of Tryptophan 2,3-dioxygenase (TDO) from Xanthomonas campestris in complex with ferrous heme and 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 | HOH491 |
B | HOH497 |
B | HOH500 |
B | HOH574 |
B | HOH744 |
B | HOH752 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 308 |
Chain | Residue |
B | HOH564 |
B | HOH596 |
B | HOH764 |
B | GLU207 |
B | HOH524 |
B | HOH551 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TRP A 307 |
Chain | Residue |
A | PHE51 |
A | HIS55 |
A | TYR113 |
A | ARG117 |
A | SER123 |
A | GLY253 |
A | THR254 |
A | HEM401 |
A | HOH402 |
B | TYR24 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE TRP A 308 |
Chain | Residue |
A | ARG85 |
A | LYS92 |
A | TYR220 |
A | SER221 |
A | GLU224 |
A | ASP228 |
A | HOH411 |
A | HOH422 |
A | HOH442 |
A | HOH502 |
A | HOH698 |
B | LYS86 |
B | ALA89 |
B | HOH536 |
B | HOH597 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TRP B 309 |
Chain | Residue |
A | TYR24 |
A | ARG215 |
B | PHE51 |
B | HIS55 |
B | TYR113 |
B | GLY121 |
B | PRO122 |
B | SER123 |
B | HOH402 |
B | HOH687 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE TRP B 310 |
Chain | Residue |
A | LYS86 |
A | ALA89 |
A | HOH495 |
A | HOH539 |
B | ARG85 |
B | LYS92 |
B | TYR220 |
B | SER221 |
B | GLU224 |
B | ASP225 |
B | ASP228 |
B | HOH411 |
B | HOH434 |
B | HOH517 |
B | HOH560 |
site_id | AC7 |
Number of Residues | 27 |
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 | ILE248 |
A | GLY253 |
A | THR254 |
A | GLY255 |
A | GLY256 |
A | SER257 |
A | GLY259 |
A | TRP307 |
A | HOH402 |
A | HOH459 |
A | HOH514 |
A | HOH534 |
A | HOH694 |
B | TYR24 |
site_id | AC8 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEM B 401 |
Chain | Residue |
B | TYR131 |
B | ARG132 |
B | HIS240 |
B | VAL244 |
B | ILE248 |
B | GLY259 |
B | HOH402 |
B | HOH489 |
B | HOH499 |
B | HOH741 |
B | HOH751 |
A | TYR24 |
A | ARG215 |
B | PHE51 |
B | GLN54 |
B | HIS55 |
B | SER58 |
B | TRP102 |
B | SER124 |
B | GLY125 |
B | PHE126 |
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 |