Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3NWL

The crystal structure of the P212121 form of bovine liver catalase previously characterized by electron microscopy

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004096	molecular_function	catalase activity
A	0004601	molecular_function	peroxidase activity
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005777	cellular_component	peroxisome
A	0005782	cellular_component	peroxisomal matrix
A	0006979	biological_process	response to oxidative stress
A	0016491	molecular_function	oxidoreductase activity
A	0019899	molecular_function	enzyme binding
A	0020037	molecular_function	heme binding
A	0042542	biological_process	response to hydrogen peroxide
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0046872	molecular_function	metal ion binding
A	0051781	biological_process	positive regulation of cell division
A	0098869	biological_process	cellular oxidant detoxification
B	0004096	molecular_function	catalase activity
B	0004601	molecular_function	peroxidase activity
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005777	cellular_component	peroxisome
B	0005782	cellular_component	peroxisomal matrix
B	0006979	biological_process	response to oxidative stress
B	0016491	molecular_function	oxidoreductase activity
B	0019899	molecular_function	enzyme binding
B	0020037	molecular_function	heme binding
B	0042542	biological_process	response to hydrogen peroxide
B	0042744	biological_process	hydrogen peroxide catabolic process
B	0046872	molecular_function	metal ion binding
B	0051781	biological_process	positive regulation of cell division
B	0098869	biological_process	cellular oxidant detoxification
C	0004096	molecular_function	catalase activity
C	0004601	molecular_function	peroxidase activity
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005777	cellular_component	peroxisome
C	0005782	cellular_component	peroxisomal matrix
C	0006979	biological_process	response to oxidative stress
C	0016491	molecular_function	oxidoreductase activity
C	0019899	molecular_function	enzyme binding
C	0020037	molecular_function	heme binding
C	0042542	biological_process	response to hydrogen peroxide
C	0042744	biological_process	hydrogen peroxide catabolic process
C	0046872	molecular_function	metal ion binding
C	0051781	biological_process	positive regulation of cell division
C	0098869	biological_process	cellular oxidant detoxification
D	0004096	molecular_function	catalase activity
D	0004601	molecular_function	peroxidase activity
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005777	cellular_component	peroxisome
D	0005782	cellular_component	peroxisomal matrix
D	0006979	biological_process	response to oxidative stress
D	0016491	molecular_function	oxidoreductase activity
D	0019899	molecular_function	enzyme binding
D	0020037	molecular_function	heme binding
D	0042542	biological_process	response to hydrogen peroxide
D	0042744	biological_process	hydrogen peroxide catabolic process
D	0046872	molecular_function	metal ion binding
D	0051781	biological_process	positive regulation of cell division
D	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEM A 527

Chain	Residue
A	ARG71
A	ALA157
A	PHE160
A	GLY215
A	SER216
A	LEU298
A	PHE333
A	MET349
A	ARG353
A	TYR357
A	THR360
A	VAL72
A	HIS361
A	ARG364
A	HOH536
A	HOH538
D	ASP64
A	VAL73
A	HIS74
A	ARG111
A	GLY130
A	VAL145
A	GLY146
A	ASN147

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE NDP A 528

Chain	Residue
A	PRO150
A	HIS193
A	PHE197
A	SER200
A	ARG202
A	ASP212
A	TYR214
A	HIS234
A	LYS236
A	VAL301
A	TRP302
A	PRO303
A	HIS304
A	GLN441
A	PHE445
A	VAL449
A	HOH560

site_id	AC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM B 527

Chain	Residue
B	ARG71
B	VAL72
B	VAL73
B	HIS74
B	ARG111
B	GLY130
B	VAL145
B	GLY146
B	ASN147
B	ALA157
B	PHE160
B	SER216
B	PHE333
B	MET349
B	ARG353
B	TYR357
B	THR360
B	HIS361
B	ARG364
B	HOH533
C	MET60
C	ASP64

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE NDP B 528

Chain	Residue
B	HIS193
B	PHE197
B	SER200
B	ARG202
B	ASP212
B	HIS234
B	LYS236
B	VAL301
B	TRP302
B	PRO303
B	HIS304
B	GLN441
B	PHE445
B	VAL449

site_id	AC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM C 527

Chain	Residue
C	HOH558
B	MET60
C	ARG71
C	VAL72
C	HIS74
C	ARG111
C	GLY130
C	VAL145
C	GLY146
C	ASN147
C	PHE160
C	GLY215
C	SER216
C	LEU298
C	PHE333
C	MET349
C	ARG353
C	ALA356
C	TYR357
C	THR360
C	HIS361
C	ARG364
C	HOH553

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE NDP C 528

Chain	Residue
C	HIS193
C	PHE197
C	SER200
C	ARG202
C	ASP212
C	HIS234
C	LYS236
C	VAL301
C	TRP302
C	HIS304
C	GLN441
C	PHE445
C	VAL449

site_id	AC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM D 527

Chain	Residue
A	MET60
D	ARG71
D	VAL72
D	VAL73
D	HIS74
D	ARG111
D	GLY130
D	VAL145
D	GLY146
D	ASN147
D	ALA157
D	PHE160
D	SER216
D	PHE333
D	MET349
D	ARG353
D	TYR357
D	THR360
D	HIS361
D	ARG364
D	HOH552

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NDP D 528

Chain	Residue
D	HIS193
D	PHE197
D	SER200
D	ARG202
D	ASP212
D	HIS234
D	LYS236
D	VAL301
D	TRP302
D	PRO303
D	HIS304
D	GLN441
D	PHE445
D	VAL449
D	HOH544
D	HOH546

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ARG353-HIS361

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

Chain	Residue	Details
A	PHE63-GLY79

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10013","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7328661","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10013","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10417406","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BLC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P04040","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10417406","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BLC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04040","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P24270","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P24270","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P24270","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P24270","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)