Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7P46

Crystal Structure of Xanthomonas campestris Tryptophan 2,3-dioxygenase (TDO)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004833molecular_functionL-tryptophan 2,3-dioxygenase activity
A0019441biological_processobsolete L-tryptophan catabolic process to L-kynurenine
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0004833molecular_functionL-tryptophan 2,3-dioxygenase activity
B0019441biological_processobsolete L-tryptophan catabolic process to L-kynurenine
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
C0004833molecular_functionL-tryptophan 2,3-dioxygenase activity
C0019441biological_processobsolete L-tryptophan catabolic process to L-kynurenine
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
D0004833molecular_functionL-tryptophan 2,3-dioxygenase activity
D0019441biological_processobsolete L-tryptophan catabolic process to L-kynurenine
D0020037molecular_functionheme binding
D0046872molecular_functionmetal ion binding
E0004833molecular_functionL-tryptophan 2,3-dioxygenase activity
E0019441biological_processobsolete L-tryptophan catabolic process to L-kynurenine
E0020037molecular_functionheme binding
E0046872molecular_functionmetal ion binding
F0004833molecular_functionL-tryptophan 2,3-dioxygenase activity
F0019441biological_processobsolete L-tryptophan catabolic process to L-kynurenine
F0020037molecular_functionheme binding
F0046872molecular_functionmetal ion binding
G0004833molecular_functionL-tryptophan 2,3-dioxygenase activity
G0019441biological_processobsolete L-tryptophan catabolic process to L-kynurenine
G0020037molecular_functionheme binding
G0046872molecular_functionmetal ion binding
H0004833molecular_functionL-tryptophan 2,3-dioxygenase activity
H0019441biological_processobsolete L-tryptophan catabolic process to L-kynurenine
H0020037molecular_functionheme binding
H0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01972","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17197414","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18783250","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2NW8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BK9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01972","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17197414","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18783250","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2NW8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BK9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3E08","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01972","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17197414","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18783250","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2NW7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NW8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NW9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BK9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3E08","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

253091

PDB entries from 2026-05-06

PDB statisticsPDBj update infoContact PDBjnumon