4HKA

Crystal structure of Drosophila melanogaster tryptophan 2,3-dioxygenase in complex with HEME

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004833	molecular_function	L-tryptophan 2,3-dioxygenase activity
A	0005829	cellular_component	cytosol
A	0006569	biological_process	L-tryptophan catabolic process
A	0006727	biological_process	ommochrome biosynthetic 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	0048072	biological_process	compound eye pigmentation
A	0051213	molecular_function	dioxygenase activity
A	0051289	biological_process	protein homotetramerization
A	0070189	biological_process	kynurenine metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM A 401

Chain	Residue
A	TYR27
A	GLN138
A	PHE142
A	TYR159
A	ASN160
A	TRP308
A	ARG309
A	HIS312
A	MET315
A	VAL316
A	MET319
A	PHE57
A	TYR335
A	LEU336
A	HOH521
A	HIS61
A	TYR64
A	PHE68
A	LEU116
A	PHE124
A	ALA134
A	PHE137

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03020","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_03020","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23333332","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4HKA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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