2NW7
Crystal Structure of Tryptophan 2,3-dioxygenase (TDO) from Xanthomonas campestris in complex with ferric heme. 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 |
C | 0004833 | molecular_function | tryptophan 2,3-dioxygenase activity |
C | 0006569 | biological_process | tryptophan catabolic process |
C | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
C | 0019442 | biological_process | tryptophan catabolic process to acetyl-CoA |
C | 0020037 | molecular_function | heme binding |
C | 0046872 | molecular_function | metal ion binding |
C | 0051213 | molecular_function | dioxygenase activity |
D | 0004833 | molecular_function | tryptophan 2,3-dioxygenase activity |
D | 0006569 | biological_process | tryptophan catabolic process |
D | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
D | 0019442 | biological_process | tryptophan catabolic process to acetyl-CoA |
D | 0020037 | molecular_function | heme binding |
D | 0046872 | molecular_function | metal ion binding |
D | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE HEM A 401 |
Chain | Residue |
A | PHE51 |
A | HIS240 |
A | VAL244 |
A | PHE262 |
A | HIS55 |
A | TRP102 |
A | LEU105 |
A | SER124 |
A | GLY125 |
A | TYR131 |
A | ARG132 |
A | TRP236 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE HEM B 401 |
Chain | Residue |
B | PHE51 |
B | HIS55 |
B | TRP102 |
B | LEU105 |
B | SER124 |
B | GLY125 |
B | PHE126 |
B | TYR131 |
B | HIS240 |
B | VAL244 |
B | GLY259 |
B | PHE262 |
B | LEU263 |
C | TYR24 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE HEM C 401 |
Chain | Residue |
C | PHE51 |
C | HIS55 |
C | LEU105 |
C | SER124 |
C | GLY125 |
C | PHE126 |
C | TYR131 |
C | ARG132 |
C | HIS240 |
C | VAL244 |
C | ILE248 |
C | PHE262 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE HEM D 401 |
Chain | Residue |
D | PHE51 |
D | HIS55 |
D | LEU105 |
D | SER124 |
D | GLY125 |
D | PHE126 |
D | TYR131 |
D | HIS240 |
D | VAL244 |
D | PHE262 |
D | LEU263 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
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 | |
C | PHE51 | |
D | PHE51 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
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 | |
D | TYR113 | |
D | ARG117 | |
D | THR254 | |
A | ARG117 | |
A | THR254 | |
B | TYR113 | |
B | ARG117 | |
B | THR254 | |
C | TYR113 | |
C | ARG117 | |
C | THR254 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
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 | |
C | HIS240 | |
D | HIS240 |