7P46

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

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
E	0004833	molecular_function	tryptophan 2,3-dioxygenase activity
E	0006569	biological_process	tryptophan catabolic process
E	0019441	biological_process	tryptophan catabolic process to kynurenine
E	0019442	biological_process	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	tryptophan 2,3-dioxygenase activity
F	0006569	biological_process	tryptophan catabolic process
F	0019441	biological_process	tryptophan catabolic process to kynurenine
F	0019442	biological_process	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	tryptophan 2,3-dioxygenase activity
G	0006569	biological_process	tryptophan catabolic process
G	0019441	biological_process	tryptophan catabolic process to kynurenine
G	0019442	biological_process	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	tryptophan 2,3-dioxygenase activity
H	0006569	biological_process	tryptophan catabolic process
H	0019441	biological_process	tryptophan catabolic process to kynurenine
H	0019442	biological_process	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	8
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
E	PHE51
F	PHE51
G	PHE51
H	PHE51

---

site_id	SWS_FT_FI2
Number of Residues	24
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
B	TYR113
B	ARG117
B	THR254
C	TYR113
C	ARG117
C	THR254
D	TYR113
D	ARG117
D	THR254
E	TYR113
E	ARG117
E	THR254
F	TYR113
F	ARG117
F	THR254
G	TYR113
G	ARG117
G	THR254
H	TYR113
H	ARG117
H	THR254
A	TYR113
A	ARG117
A	THR254

---

site_id	SWS_FT_FI3
Number of Residues	8
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
E	HIS240
F	HIS240
G	HIS240
H	HIS240

---