Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4BLC

THE STRUCTURE OF ORTHORHOMBIC CRYSTALS OF BEEF LIVER CATALASE

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	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	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	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	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	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	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	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	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	21
Details	BINDING SITE FOR RESIDUE HEM A 507

Chain	Residue
A	GLY130
A	VAL145
A	GLY146
A	ASN147
A	PHE160
A	GLY215
A	SER216
A	PHE333
A	MET349
A	ARG353
A	TYR357
A	THR360
A	HIS361
A	ARG364
A	HOH705
A	HOH744
A	ARG71
A	VAL72
A	VAL73
A	HIS74
A	ARG111

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE NDP A 1102

Chain	Residue
A	PRO150
A	HIS193
A	PHE197
A	ARG202
A	ASP212
A	TYR214
A	LYS236
A	VAL301
A	TRP302
A	PRO303
A	HIS304
A	GLN441
A	THR444
A	PHE445
A	VAL449
A	HOH862
D	GLU453

site_id	AC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM B 507

Chain	Residue
B	ARG71
B	VAL73
B	HIS74
B	ARG111
B	VAL145
B	GLY146
B	ASN147
B	PHE152
B	ALA157
B	PHE160
B	SER216
B	LEU298
B	PHE333
B	MET349
B	ARG353
B	TYR357
B	THR360
B	HIS361
B	ARG364
B	HOH961
C	MET60

site_id	AC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE NDP B 1202

Chain	Residue
B	HIS193
B	PHE197
B	SER200
B	ARG202
B	ASP212
B	TYR214
B	HIS234
B	LYS236
B	ILE241
B	VAL301
B	TRP302
B	PRO303
B	HIS304
B	GLN441
B	THR444
B	PHE445
B	VAL449
B	LEU450

site_id	AC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM C 507

Chain	Residue
C	ARG353
C	TYR357
C	HIS361
C	ARG364
C	HOH804
B	MET60
B	ASP64
C	ARG71
C	VAL72
C	VAL73
C	HIS74
C	ARG111
C	GLY130
C	VAL145
C	GLY146
C	ASN147
C	PHE160
C	GLY215
C	SER216
C	HIS217
C	LEU298
C	PHE333
C	MET349

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE NDP C 1302

Chain	Residue
C	PRO150
C	HIS193
C	PHE197
C	ARG202
C	ASP212
C	TYR214
C	LYS236
C	TRP302
C	PRO303
C	HIS304
C	GLN441
C	THR444
C	PHE445
C	VAL449
C	HOH801

site_id	AC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM D 507

Chain	Residue
A	MET60
D	ARG71
D	VAL72
D	VAL73
D	HIS74
D	ARG111
D	VAL145
D	GLY146
D	ASN147
D	ALA157
D	PHE160
D	PHE333
D	MET349
D	ARG353
D	ALA356
D	TYR357
D	HIS361
D	ARG364
D	HOH838

site_id	AC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NDP D 1402

Chain	Residue
A	GLU453
D	HIS193
D	PHE197
D	SER200
D	ARG202
D	ASP212
D	TYR214
D	HIS234
D	LYS236
D	VAL301
D	TRP302
D	PRO303
D	HIS304
D	GLN441
D	THR444
D	PHE445
D	LEU450
D	HOH1024
D	HOH1080

site_id	CAT
Number of Residues	4
Details	THE IRON OF HEME GROUP IS THE ACTIVE CENTER WHICH BINDS SUBSTRATE H2O2.

Chain	Residue
A	HEM507
B	HEM507
C	HEM507
D	HEM507

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
A	ALA75
B	ALA75
C	ALA75
D	ALA75

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

Chain	Residue	Details
A	ASN148
B	ASN148
C	ASN148
D	ASN148

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

Chain	Residue	Details
A	GLN194
A	PHE445
A	TYR446
B	GLN194
B	LEU198
B	ASP201
B	GLY203
B	GLY215
B	THR237
B	PRO303
B	GLY305
A	LEU198
B	VAL442
B	PHE445
B	TYR446
C	GLN194
C	LEU198
C	ASP201
C	GLY203
C	GLY215
C	THR237
C	PRO303
A	ASP201
C	GLY305
C	VAL442
C	PHE445
C	TYR446
D	GLN194
D	LEU198
D	ASP201
D	GLY203
D	GLY215
D	THR237
A	GLY203
D	PRO303
D	GLY305
D	VAL442
D	PHE445
D	TYR446
A	GLY215
A	THR237
A	PRO303
A	GLY305
A	VAL442

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

Chain	Residue	Details
A	GLY213
B	GLY213
C	GLY213
D	GLY213

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
A	PRO358
B	PRO358
C	PRO358
D	PRO358

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

Chain	Residue	Details
A	ASP2
B	ASP2
C	ASP2
D	ASP2

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P04040

Chain	Residue	Details
A	ASP9
B	ASP9
C	ASP9
D	ASP9

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

Chain	Residue	Details
A	HIS13
A	LEU221
B	HIS13
B	LEU221
C	HIS13
C	LEU221
D	HIS13
D	LEU221

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

Chain	Residue	Details
A	PHE233
A	TYR499
B	PHE233
B	TYR499
C	PHE233
C	TYR499
D	PHE233
D	TYR499

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

Chain	Residue	Details
A	ALA417
A	ALA434
B	ALA417
B	ALA434
C	ALA417
C	ALA434
D	ALA417
D	ALA434

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

Chain	Residue	Details
A	VAL449
A	ASN480
B	VAL449
B	ASN480
C	VAL449
C	ASN480
D	VAL449
D	ASN480

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)