2IUF

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004096	molecular_function	catalase activity
A	0004601	molecular_function	peroxidase activity
A	0005829	cellular_component	cytosol
A	0006979	biological_process	response to oxidative stress
A	0016491	molecular_function	oxidoreductase activity
A	0020037	molecular_function	heme binding
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0046872	molecular_function	metal ion binding
A	0070301	biological_process	cellular response to hydrogen peroxide
A	0098869	biological_process	cellular oxidant detoxification
E	0004096	molecular_function	catalase activity
E	0004601	molecular_function	peroxidase activity
E	0005829	cellular_component	cytosol
E	0006979	biological_process	response to oxidative stress
E	0016491	molecular_function	oxidoreductase activity
E	0020037	molecular_function	heme binding
E	0042744	biological_process	hydrogen peroxide catabolic process
E	0046872	molecular_function	metal ion binding
E	0070301	biological_process	cellular response to hydrogen peroxide
E	0098869	biological_process	cellular oxidant detoxification

Functional Information from PROSITE/UniProt

site_id	PS00437
Number of Residues	9
Details	CATALASE_1 Catalase proximal heme-ligand signature. RLFSYlDTQ

Chain	Residue	Details
A	ARG347-GLN355

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site_id	PS00438
Number of Residues	17
Details	CATALASE_2 Catalase proximal active site signature. FdHervpERavHarGTG

Chain	Residue	Details
A	PHE53-GLY69

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1iph

Chain	Residue	Details
A	SER103
A	HIS64
A	ASN137

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site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1iph

Chain	Residue	Details
E	SER103
E	HIS64
E	ASN137

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