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9FW4

Crystal structure of Heme-Oxygenase mutant H20C from Corynebacterium diphtheriae complexed with Cobalt-porphyrine (HumO-Co(III))

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
Functional Information from PROSITE/UniProt
site_idPS00593
Number of Residues11
DetailsHEME_OXYGENASE Heme oxygenase signature. LVAHHYVRYLG
ChainResidueDetails
ALEU125-GLY135

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 795
ChainResidueDetails
AHIS25metal ligand
ATYR53activator, electrostatic stabiliser
AVAL131activator
AARG132activator
AGLY135steric role
AASP136modifies pKa
AGLY140steric role

site_idMCSA2
Number of Residues7
DetailsM-CSA 795
ChainResidueDetails
BHIS25metal ligand
BTYR53activator, electrostatic stabiliser
BVAL131activator
BARG132activator
BGLY135steric role
BASP136modifies pKa
BGLY140steric role

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PDB entries from 2026-01-28

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