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4GPC

Structure of the biliverdin-HmuO, heme oxygenase from Corynebacterium diphtheriae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004392molecular_functionheme oxygenase (decyclizing) activity
A0006788biological_processheme oxidation
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0042167biological_processheme catabolic process
A0046872molecular_functionmetal ion binding
B0004392molecular_functionheme oxygenase (decyclizing) activity
B0006788biological_processheme oxidation
B0006979biological_processresponse to oxidative stress
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0042167biological_processheme catabolic process
B0046872molecular_functionmetal ion binding
C0004392molecular_functionheme oxygenase (decyclizing) activity
C0006788biological_processheme oxidation
C0006979biological_processresponse to oxidative stress
C0016491molecular_functionoxidoreductase activity
C0020037molecular_functionheme binding
C0042167biological_processheme catabolic process
C0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00593
Number of Residues11
DetailsHEME_OXYGENASE Heme oxygenase signature. LVAHHYVRYLG
ChainResidueDetails
ALEU125-GLY135

246704

PDB entries from 2025-12-24

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