7P46

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004833	molecular_function	L-tryptophan 2,3-dioxygenase activity
A	0006569	biological_process	L-tryptophan catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0019441	biological_process	L-tryptophan catabolic process to kynurenine
A	0019442	biological_process	L-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	L-tryptophan 2,3-dioxygenase activity
B	0006569	biological_process	L-tryptophan catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0019441	biological_process	L-tryptophan catabolic process to kynurenine
B	0019442	biological_process	L-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	L-tryptophan 2,3-dioxygenase activity
C	0006569	biological_process	L-tryptophan catabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0019441	biological_process	L-tryptophan catabolic process to kynurenine
C	0019442	biological_process	L-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	L-tryptophan 2,3-dioxygenase activity
D	0006569	biological_process	L-tryptophan catabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0019441	biological_process	L-tryptophan catabolic process to kynurenine
D	0019442	biological_process	L-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
E	0004833	molecular_function	L-tryptophan 2,3-dioxygenase activity
E	0006569	biological_process	L-tryptophan catabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0019441	biological_process	L-tryptophan catabolic process to kynurenine
E	0019442	biological_process	L-tryptophan catabolic process to acetyl-CoA
E	0020037	molecular_function	heme binding
E	0046872	molecular_function	metal ion binding
E	0051213	molecular_function	dioxygenase activity
F	0004833	molecular_function	L-tryptophan 2,3-dioxygenase activity
F	0006569	biological_process	L-tryptophan catabolic process
F	0016491	molecular_function	oxidoreductase activity
F	0019441	biological_process	L-tryptophan catabolic process to kynurenine
F	0019442	biological_process	L-tryptophan catabolic process to acetyl-CoA
F	0020037	molecular_function	heme binding
F	0046872	molecular_function	metal ion binding
F	0051213	molecular_function	dioxygenase activity
G	0004833	molecular_function	L-tryptophan 2,3-dioxygenase activity
G	0006569	biological_process	L-tryptophan catabolic process
G	0016491	molecular_function	oxidoreductase activity
G	0019441	biological_process	L-tryptophan catabolic process to kynurenine
G	0019442	biological_process	L-tryptophan catabolic process to acetyl-CoA
G	0020037	molecular_function	heme binding
G	0046872	molecular_function	metal ion binding
G	0051213	molecular_function	dioxygenase activity
H	0004833	molecular_function	L-tryptophan 2,3-dioxygenase activity
H	0006569	biological_process	L-tryptophan catabolic process
H	0016491	molecular_function	oxidoreductase activity
H	0019441	biological_process	L-tryptophan catabolic process to kynurenine
H	0019442	biological_process	L-tryptophan catabolic process to acetyl-CoA
H	0020037	molecular_function	heme binding
H	0046872	molecular_function	metal ion binding
H	0051213	molecular_function	dioxygenase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	32
Details	Binding 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"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding 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"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding 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"}]}

Chain

Residue

Details

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