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2IUF

The structures of Penicillium vitale catalase: resting state, oxidised state (compound I) and complex with aminotriazole

Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
E0004096molecular_functioncatalase activity
E0004601molecular_functionperoxidase activity
E0005829cellular_componentcytosol
E0006979biological_processresponse to oxidative stress
E0016491molecular_functionoxidoreductase activity
E0020037molecular_functionheme binding
E0042744biological_processhydrogen peroxide catabolic process
E0046872molecular_functionmetal ion binding
E0098869biological_processcellular oxidant detoxification
Functional Information from PROSITE/UniProt
site_idPS00437
Number of Residues9
DetailsCATALASE_1 Catalase proximal heme-ligand signature. RLFSYlDTQ
ChainResidueDetails
AARG347-GLN355

site_idPS00438
Number of Residues17
DetailsCATALASE_2 Catalase proximal active site signature. FdHervpERavHarGTG
ChainResidueDetails
APHE53-GLY69

218853

PDB entries from 2024-04-24

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