Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1TH3

Crystal structure of NADPH depleted bovine live catalase complexed with cyanide

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	5
Details	BINDING SITE FOR RESIDUE CYN A 3000

Chain	Residue
A	HIS74
A	PHE160
A	TYR357
A	HEM2000
A	HOH3009

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CYN D 3001

Chain	Residue
D	HOH3155
D	VAL73
D	HIS74
D	PHE160
D	HEM2003

site_id	AC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM A 2000

Chain	Residue
A	ARG71
A	VAL72
A	VAL73
A	HIS74
A	ARG111
A	VAL145
A	GLY146
A	ASN147
A	PHE160
A	HIS217
A	LEU298
A	PHE333
A	MET349
A	ARG353
A	TYR357
A	HIS361
A	ARG364
A	CYN3000
A	HOH3003
A	HOH3016
D	ASP64

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM B 2001

Chain	Residue
B	ARG71
B	HIS74
B	ARG111
B	VAL145
B	GLY146
B	ASN147
B	PHE160
B	SER216
B	HIS217
B	PHE333
B	MET349
B	ARG353
B	TYR357
B	THR360
B	HIS361
B	ARG364
B	HOH2003
B	HOH2179
C	ASP64

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM C 2002

Chain	Residue
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	PHE333
C	MET349
C	ARG353
C	TYR357
C	THR360
C	HIS361
C	ARG364

site_id	AC6
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM D 2003

Chain	Residue
A	MET60
A	ASP64
D	ARG71
D	VAL73
D	HIS74
D	ARG111
D	VAL145
D	GLY146
D	ASN147
D	PHE160
D	SER216
D	HIS217
D	LEU298
D	PHE333
D	MET349
D	ARG353
D	TYR357
D	HIS361
D	ARG364
D	CYN3001
D	HOH3012
D	HOH3155

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

Catalytic Information from CSA

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

Chain	Residue	Details
A	SER113
A	HIS74
A	ASN147

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

Chain	Residue	Details
B	SER113
B	HIS74
B	ASN147

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1iph

Chain	Residue	Details
C	SER113
C	HIS74
C	ASN147

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1iph

Chain	Residue	Details
D	SER113
D	HIS74
D	ASN147

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