8QV7

Crystal structure of human TDO with alpha-methyl-L-tryptophan

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004833	molecular_function	tryptophan 2,3-dioxygenase activity
A	0019441	biological_process	L-tryptophan catabolic process to kynurenine
A	0020037	molecular_function	heme binding
A	0046872	molecular_function	metal ion binding
B	0004833	molecular_function	tryptophan 2,3-dioxygenase activity
B	0019441	biological_process	L-tryptophan catabolic process to kynurenine
B	0020037	molecular_function	heme binding
B	0046872	molecular_function	metal ion binding
C	0004833	molecular_function	tryptophan 2,3-dioxygenase activity
C	0019441	biological_process	L-tryptophan catabolic process to kynurenine
C	0020037	molecular_function	heme binding
C	0046872	molecular_function	metal ion binding
D	0004833	molecular_function	tryptophan 2,3-dioxygenase activity
D	0019441	biological_process	L-tryptophan catabolic process to kynurenine
D	0020037	molecular_function	heme binding
D	0046872	molecular_function	metal ion binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03020","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27762317","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5TI9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_03020","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27762317","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5TI9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---