Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4E37

Crystal Structure of P. aeruginosa catalase, KatA tetramer

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	0006979	biological_process	response to oxidative stress
A	0016491	molecular_function	oxidoreductase activity
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	0098869	biological_process	cellular oxidant detoxification
B	0004096	molecular_function	catalase activity
B	0004601	molecular_function	peroxidase activity
B	0005737	cellular_component	cytoplasm
B	0006979	biological_process	response to oxidative stress
B	0016491	molecular_function	oxidoreductase activity
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	0098869	biological_process	cellular oxidant detoxification
C	0004096	molecular_function	catalase activity
C	0004601	molecular_function	peroxidase activity
C	0005737	cellular_component	cytoplasm
C	0006979	biological_process	response to oxidative stress
C	0016491	molecular_function	oxidoreductase activity
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	0098869	biological_process	cellular oxidant detoxification
D	0004096	molecular_function	catalase activity
D	0004601	molecular_function	peroxidase activity
D	0005737	cellular_component	cytoplasm
D	0006979	biological_process	response to oxidative stress
D	0016491	molecular_function	oxidoreductase activity
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	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 500

Chain	Residue
A	ARG52
A	PHE141
A	SER197
A	HIS198
A	PHE314
A	MET330
A	ARG334
A	SER337
A	TYR338
A	HIS342
A	ARG345
A	HIS55
A	HOH619
A	HOH621
A	HOH628
A	HOH697
B	ASP45
A	ARG92
A	GLY111
A	PHE112
A	VAL126
A	GLY127
A	ASN128
A	PRO138

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NDP A 501

Chain	Residue
A	PRO131
A	HIS174
A	SER181
A	ARG183
A	HIS193
A	HIS215
A	VAL282
A	TRP283
A	PRO284
A	HIS285
A	GLN423
A	LEU427
A	LEU430
A	PHE431
A	HOH709
A	HOH717

site_id	AC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM B 500

Chain	Residue
A	ASP45
B	ARG52
B	HIS55
B	ARG92
B	GLY111
B	PHE112
B	VAL126
B	GLY127
B	ASN128
B	PRO138
B	PHE141
B	SER197
B	HIS198
B	PHE314
B	MET330
B	ARG334
B	SER337
B	TYR338
B	HIS342
B	ARG345
B	HOH621
B	HOH641
B	HOH679

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NDP B 501

Chain	Residue
B	PRO131
B	HIS174
B	SER181
B	ARG183
B	HIS193
B	HIS215
B	VAL282
B	TRP283
B	PRO284
B	HIS285
B	GLN423
B	ALA426
B	LEU427
B	LEU430
B	PHE431
B	HOH705

site_id	AC5
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEM C 500

Chain	Residue
C	HOH607
C	HOH628
C	HOH670
D	ASP45
C	ARG52
C	HIS55
C	ARG92
C	GLY111
C	PHE112
C	VAL126
C	GLY127
C	ASN128
C	PRO138
C	PHE141
C	SER197
C	HIS198
C	PHE314
C	MET330
C	ARG334
C	SER337
C	TYR338
C	HIS342
C	ARG345
C	HOH604

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE NDP C 501

Chain	Residue
C	PRO131
C	HIS174
C	SER181
C	ARG183
C	HIS193
C	HIS215
C	VAL282
C	TRP283
C	PRO284
C	HIS285
C	GLN423
C	LEU427
C	LEU430
C	PHE431
C	HOH699

site_id	AC7
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM D 500

Chain	Residue
D	ARG52
D	OMT54
D	HIS55
D	ARG92
D	VAL126
D	GLY127
D	ASN128
D	PRO138
D	PHE141
D	GLY196
D	SER197
D	HIS198
D	PHE314
D	MET330
D	ARG334
D	SER337
D	TYR338
D	HIS342
D	ARG345
D	HOH615
D	HOH627
D	HOH638

site_id	AC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE NDP D 501

Chain	Residue
D	PRO131
D	HIS174
D	SER181
D	ARG183
D	HIS193
D	HIS215
D	VAL282
D	TRP283
D	PRO284
D	HIS285
D	GLN423
D	LEU427
D	PHE431
D	HOH613

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ARG334-HIS342

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

Chain	Residue	Details
A	PHE44-ALA60

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:0000305\|PubMed:24663218

Chain	Residue	Details
A	HIS55
B	HIS55
C	HIS55
D	HIS55

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

Chain	Residue	Details
A	ASN128
B	ASN128
C	ASN128
D	ASN128

site_id	SWS_FT_FI3
Number of Residues	48
Details	BINDING: BINDING => ECO:0007744\|PDB:4E37

Chain	Residue	Details
A	ARG52
A	HIS342
A	ARG345
A	GLN423
B	ARG52
B	ARG92
B	PHE141
B	HIS174
B	SER181
B	ARG183
B	HIS193
A	ARG92
B	TRP283
B	HIS285
B	HIS342
B	ARG345
B	GLN423
C	ARG52
C	ARG92
C	PHE141
C	HIS174
C	SER181
A	PHE141
C	ARG183
C	HIS193
C	TRP283
C	HIS285
C	HIS342
C	ARG345
C	GLN423
D	ARG52
D	ARG92
D	PHE141
A	HIS174
D	HIS174
D	SER181
D	ARG183
D	HIS193
D	TRP283
D	HIS285
D	HIS342
D	ARG345
D	GLN423
A	SER181
A	ARG183
A	HIS193
A	TRP283
A	HIS285

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: axial binding residue => ECO:0000269\|PubMed:24663218, ECO:0007744\|PDB:4E37

Chain	Residue	Details
A	TYR338
B	TYR338
C	TYR338
D	TYR338

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