3MOO

Crystal structure of the HmuO, heme oxygenase from Corynebacterium diphtheriae, in complex with azide-bound verdoheme

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004392	molecular_function	heme oxygenase (decyclizing) activity
A	0006788	biological_process	heme oxidation
A	0006979	biological_process	response to oxidative stress
A	0016491	molecular_function	oxidoreductase activity
A	0020037	molecular_function	heme binding
A	0042167	biological_process	heme catabolic process
A	0046872	molecular_function	metal ion binding
B	0004392	molecular_function	heme oxygenase (decyclizing) activity
B	0006788	biological_process	heme oxidation
B	0006979	biological_process	response to oxidative stress
B	0016491	molecular_function	oxidoreductase activity
B	0020037	molecular_function	heme binding
B	0042167	biological_process	heme catabolic process
B	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00593
Number of Residues	11
Details	HEME_OXYGENASE Heme oxygenase signature. LVAHHYVRYLG

Chain	Residue	Details
A	LEU125-GLY135

---