Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6JNT

Catalase structure determined by eEFD (dataset 1)

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	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	0061692	biological_process	cellular detoxification of hydrogen peroxide
A	0062151	cellular_component	catalase complex
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	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	0061692	biological_process	cellular detoxification of hydrogen peroxide
B	0062151	cellular_component	catalase complex
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	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	0061692	biological_process	cellular detoxification of hydrogen peroxide
C	0062151	cellular_component	catalase complex
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	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	0061692	biological_process	cellular detoxification of hydrogen peroxide
D	0062151	cellular_component	catalase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	binding site for residue HEM A 601

Chain	Residue
A	ARG71
A	SER216
A	HIS217
A	LEU298
A	PHE333
A	MET349
A	ARG353
A	TYR357
A	HIS361
A	ARG364
D	MET60
A	VAL72
D	ASP64
A	VAL73
A	HIS74
A	ARG111
A	GLY130
A	ASN147
A	ALA157
A	PHE160

site_id	AC2
Number of Residues	14
Details	binding site for residue NDP A 602

Chain	Residue
A	PRO150
A	HIS193
A	PHE197
A	SER200
A	ARG202
A	ASN212
A	LYS236
A	VAL301
A	TRP302
A	PRO303
A	HIS304
A	GLN441
A	PHE445
A	VAL449

site_id	AC3
Number of Residues	22
Details	binding site for residue HEM B 601

Chain	Residue
B	ARG71
B	VAL72
B	VAL73
B	HIS74
B	ARG111
B	ALA132
B	VAL145
B	GLY146
B	ASN147
B	ALA157
B	PHE160
B	SER216
B	HIS217
B	PHE333
B	MET349
B	ARG353
B	TYR357
B	THR360
B	HIS361
B	ARG364
C	MET60
C	ASP64

site_id	AC4
Number of Residues	14
Details	binding site for residue NDP B 602

Chain	Residue
B	HIS193
B	PHE197
B	SER200
B	ARG202
B	ASN212
B	HIS234
B	LYS236
B	VAL301
B	TRP302
B	PRO303
B	HIS304
B	GLN441
B	PHE445
B	VAL449

site_id	AC5
Number of Residues	20
Details	binding site for residue HEM C 601

Chain	Residue
B	MET60
C	ARG71
C	VAL72
C	HIS74
C	ARG111
C	GLY130
C	VAL145
C	GLY146
C	ASN147
C	PHE160
C	SER216
C	HIS217
C	PHE333
C	MET349
C	ARG353
C	ALA356
C	TYR357
C	THR360
C	HIS361
C	ARG364

site_id	AC6
Number of Residues	15
Details	binding site for residue NDP C 602

Chain	Residue
C	TRP302
C	HIS304
C	GLN441
C	PHE445
C	VAL449
C	HOH703
C	PRO150
C	HIS193
C	PHE197
C	SER200
C	ARG202
C	ASN212
C	HIS234
C	LYS236
C	VAL301

site_id	AC7
Number of Residues	20
Details	binding site for residue HEM D 601

Chain	Residue
A	MET60
D	ARG71
D	VAL72
D	VAL73
D	HIS74
D	ARG111
D	GLY130
D	VAL145
D	ASN147
D	ALA157
D	PHE160
D	SER216
D	HIS217
D	PHE333
D	MET349
D	ARG353
D	TYR357
D	THR360
D	HIS361
D	ARG364

site_id	AC8
Number of Residues	13
Details	binding site for residue NDP D 602

Chain	Residue
D	HIS193
D	PHE197
D	SER200
D	ARG202
D	ASN212
D	LYS236
D	VAL301
D	TRP302
D	HIS304
D	GLN441
D	PHE445
D	VAL449
D	HOH704

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	ACT_SITE: ACT_SITE => ECO:0000255\|PROSITE-ProRule:PRU10013, ECO:0000269\|PubMed:7328661

Chain	Residue	Details
C	HIS74
D	HIS74
A	HIS74
B	HIS74

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000255\|PROSITE-ProRule:PRU10013

Chain	Residue	Details
B	ASN147
C	ASN147
D	ASN147
A	ASN147

site_id	SWS_FT_FI3
Number of Residues	44
Details	BINDING: BINDING => ECO:0000269\|PubMed:10417406, ECO:0007744\|PDB:4BLC

Chain	Residue	Details
A	TYR214
A	LYS236
A	TRP302
A	HIS304
A	GLN441
A	THR444
A	PHE445
B	HIS193
B	PHE197
B	SER200
B	ARG202
B	TYR214
B	LYS236
B	TRP302
B	HIS304
B	GLN441
B	THR444
B	PHE445
C	HIS193
C	PHE197
C	SER200
C	ARG202
C	TYR214
C	LYS236
C	TRP302
C	HIS304
C	GLN441
C	THR444
C	PHE445
D	HIS193
D	PHE197
D	SER200
D	ARG202
D	TYR214
D	LYS236
D	TRP302
D	HIS304
D	GLN441
D	THR444
D	PHE445
A	SER200
A	PHE197
A	ARG202
A	HIS193

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P04040

Chain	Residue	Details
B	ASN212
C	ASN212
D	ASN212
A	ASN212

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: axial binding residue => ECO:0000269\|PubMed:10417406, ECO:0007744\|PDB:4BLC

Chain	Residue	Details
B	TYR357
C	TYR357
D	TYR357
A	TYR357

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: N-acetylalanine; alternate => ECO:0000250\|UniProtKB:P04040

Chain	Residue	Details
B	ALA1
C	ALA1
D	ALA1
A	ALA1

site_id	SWS_FT_FI7
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P04040

Chain	Residue	Details
A	SER8
A	SER516
B	SER8
B	SER516
C	SER8
C	SER516
D	SER8
D	SER516

site_id	SWS_FT_FI8
Number of Residues	8
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:P24270

Chain	Residue	Details
A	LYS12
A	LYS220
B	LYS12
B	LYS220
C	LYS12
C	LYS220
D	LYS12
D	LYS220

site_id	SWS_FT_FI9
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P24270

Chain	Residue	Details
A	LYS232
A	LYS498
B	LYS232
B	LYS498
C	LYS232
C	LYS498
D	LYS232
D	LYS498

site_id	SWS_FT_FI10
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P24270

Chain	Residue	Details
C	SER416
C	SER433
D	SER416
D	SER433
A	SER416
A	SER433
B	SER416
B	SER433

site_id	SWS_FT_FI11
Number of Residues	8
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P24270

Chain	Residue	Details
A	LYS448
A	LYS479
B	LYS448
B	LYS479
C	LYS448
C	LYS479
D	LYS448
D	LYS479

site_id	SWS_FT_FI12
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P04040

Chain	Residue	Details
A	THR510
B	THR510
C	THR510
D	THR510

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