Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1ATJ

RECOMBINANT HORSERADISH PEROXIDASE C1A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004601	molecular_function	peroxidase activity
A	0005576	cellular_component	extracellular region
A	0005773	cellular_component	vacuole
A	0006979	biological_process	response to oxidative stress
A	0016491	molecular_function	oxidoreductase activity
A	0020037	molecular_function	heme binding
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0046872	molecular_function	metal ion binding
A	0098869	biological_process	cellular oxidant detoxification
A	0140825	molecular_function	lactoperoxidase activity
B	0004601	molecular_function	peroxidase activity
B	0005576	cellular_component	extracellular region
B	0005773	cellular_component	vacuole
B	0006979	biological_process	response to oxidative stress
B	0016491	molecular_function	oxidoreductase activity
B	0020037	molecular_function	heme binding
B	0042744	biological_process	hydrogen peroxide catabolic process
B	0046872	molecular_function	metal ion binding
B	0098869	biological_process	cellular oxidant detoxification
B	0140825	molecular_function	lactoperoxidase activity
C	0004601	molecular_function	peroxidase activity
C	0005576	cellular_component	extracellular region
C	0005773	cellular_component	vacuole
C	0006979	biological_process	response to oxidative stress
C	0016491	molecular_function	oxidoreductase activity
C	0020037	molecular_function	heme binding
C	0042744	biological_process	hydrogen peroxide catabolic process
C	0046872	molecular_function	metal ion binding
C	0098869	biological_process	cellular oxidant detoxification
C	0140825	molecular_function	lactoperoxidase activity
D	0004601	molecular_function	peroxidase activity
D	0005576	cellular_component	extracellular region
D	0005773	cellular_component	vacuole
D	0006979	biological_process	response to oxidative stress
D	0016491	molecular_function	oxidoreductase activity
D	0020037	molecular_function	heme binding
D	0042744	biological_process	hydrogen peroxide catabolic process
D	0046872	molecular_function	metal ion binding
D	0098869	biological_process	cellular oxidant detoxification
D	0140825	molecular_function	lactoperoxidase activity
E	0004601	molecular_function	peroxidase activity
E	0005576	cellular_component	extracellular region
E	0005773	cellular_component	vacuole
E	0006979	biological_process	response to oxidative stress
E	0016491	molecular_function	oxidoreductase activity
E	0020037	molecular_function	heme binding
E	0042744	biological_process	hydrogen peroxide catabolic process
E	0046872	molecular_function	metal ion binding
E	0098869	biological_process	cellular oxidant detoxification
E	0140825	molecular_function	lactoperoxidase activity
F	0004601	molecular_function	peroxidase activity
F	0005576	cellular_component	extracellular region
F	0005773	cellular_component	vacuole
F	0006979	biological_process	response to oxidative stress
F	0016491	molecular_function	oxidoreductase activity
F	0020037	molecular_function	heme binding
F	0042744	biological_process	hydrogen peroxide catabolic process
F	0046872	molecular_function	metal ion binding
F	0098869	biological_process	cellular oxidant detoxification
F	0140825	molecular_function	lactoperoxidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 351

Chain	Residue
A	THR171
A	ASP222
A	THR225
A	ILE228
A	ASP230

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 352

Chain	Residue
A	SER52
A	HOH366
A	ASP43
A	VAL46
A	GLY48
A	ASP50

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 351

Chain	Residue
B	THR171
B	ASP222
B	THR225
B	ILE228
B	ASP230

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 352

Chain	Residue
B	ASP43
B	VAL46
B	GLY48
B	ASP50
B	SER52
B	HOH368

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 351

Chain	Residue
C	THR171
C	ASP222
C	THR225
C	ILE228
C	ASP230

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 352

Chain	Residue
C	ASP43
C	VAL46
C	GLY48
C	ASP50
C	SER52
C	HOH367

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 351

Chain	Residue
D	THR171
D	ASP222
D	THR225
D	ILE228
D	ASP230

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 352

Chain	Residue
D	ASP43
D	VAL46
D	GLY48
D	ASP50
D	SER52
D	HOH368

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 351

Chain	Residue
E	THR171
E	ASP222
E	THR225
E	ILE228
E	ASP230

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 352

Chain	Residue
E	ASP43
E	VAL46
E	GLY48
E	ASP50
E	SER52
E	HOH368

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA F 351

Chain	Residue
F	THR171
F	ASP222
F	THR225
F	ILE228
F	ASP230

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA F 352

Chain	Residue
F	ASP43
F	VAL46
F	GLY48
F	ASP50
F	SER52
F	HOH367

site_id	BC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM A 350

Chain	Residue
A	ARG31
A	ALA34
A	SER35
A	ARG38
A	PHE41
A	SER73
A	ALA140
A	PRO141
A	LEU166
A	GLY169
A	HIS170
A	PHE172
A	GLY173
A	LYS174
A	ASN175
A	GLN176
A	PHE179
A	PHE221
A	SER246
A	HOH391

site_id	BC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM B 350

Chain	Residue
B	LYS174
B	ASN175
B	GLN176
B	PHE179
B	PHE221
B	SER246
B	HOH393
B	ARG31
B	ALA34
B	SER35
B	ARG38
B	PHE41
B	SER73
B	ALA140
B	PRO141
B	LEU166
B	GLY169
B	HIS170
B	PHE172
B	GLY173

site_id	BC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM C 350

Chain	Residue
C	ARG31
C	ALA34
C	SER35
C	ARG38
C	PHE41
C	SER73
C	ALA140
C	PRO141
C	LEU166
C	GLY169
C	HIS170
C	PHE172
C	GLY173
C	LYS174
C	ASN175
C	GLN176
C	PHE179
C	PHE221
C	SER246
C	HOH392

site_id	BC7
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM D 350

Chain	Residue
D	ARG31
D	ALA34
D	SER35
D	ARG38
D	PHE41
D	SER73
D	ALA140
D	PRO141
D	LEU166
D	GLY169
D	HIS170
D	PHE172
D	GLY173
D	LYS174
D	ASN175
D	GLN176
D	PHE179
D	PHE221
D	SER246
D	HOH393

site_id	BC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM E 350

Chain	Residue
E	ARG31
E	ALA34
E	SER35
E	ARG38
E	PHE41
E	SER73
E	ALA140
E	PRO141
E	LEU166
E	GLY169
E	HIS170
E	PHE172
E	GLY173
E	LYS174
E	ASN175
E	GLN176
E	PHE179
E	PHE221
E	SER246
E	HOH393

site_id	BC9
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM F 350

Chain	Residue
F	ARG31
F	ALA34
F	SER35
F	ARG38
F	PHE41
F	SER73
F	ALA140
F	PRO141
F	LEU166
F	GLY169
F	HIS170
F	PHE172
F	GLY173
F	LYS174
F	ASN175
F	GLN176
F	PHE179
F	PHE221
F	SER246
F	HOH392

Functional Information from PROSITE/UniProt

site_id	PS00435
Number of Residues	11
Details	PEROXIDASE_1 Peroxidases proximal heme-ligand signature. DLVALSGGHTF

Chain	Residue	Details
A	ASP162-PHE172

site_id	PS00436
Number of Residues	12
Details	PEROXIDASE_2 Peroxidases active site signature. AAsiLRLhFHDC

Chain	Residue	Details
A	ALA33-CYS44

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	66
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Site: {"description":"Transition state stabilizer"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Modified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1001465","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	12
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"1001465","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	36
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 7atj

Chain	Residue	Details
A	ARG38
A	HIS42
A	ASN70

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 7atj

Chain	Residue	Details
B	ARG38
B	HIS42
B	ASN70

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 7atj

Chain	Residue	Details
C	ARG38
C	HIS42
C	ASN70

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 7atj

Chain	Residue	Details
D	ARG38
D	HIS42
D	ASN70

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 7atj

Chain	Residue	Details
E	ARG38
E	HIS42
E	ASN70

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 7atj

Chain	Residue	Details
F	ARG38
F	HIS42
F	ASN70

site_id	MCSA1
Number of Residues	4
Details	M-CSA 239

Chain	Residue	Details
A	ARG38	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS42	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASN70	electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity
A	HIS170	metal ligand

site_id	MCSA2
Number of Residues	4
Details	M-CSA 239

Chain	Residue	Details
B	ARG38	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	HIS42	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ASN70	electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity
B	HIS170	metal ligand

site_id	MCSA3
Number of Residues	4
Details	M-CSA 239

Chain	Residue	Details
C	ARG38	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	HIS42	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ASN70	electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity
C	HIS170	metal ligand

site_id	MCSA4
Number of Residues	4
Details	M-CSA 239

Chain	Residue	Details
D	ARG38	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	HIS42	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	ASN70	electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity
D	HIS170	metal ligand

site_id	MCSA5
Number of Residues	4
Details	M-CSA 239

Chain	Residue	Details
E	ARG38	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	HIS42	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	ASN70	electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity
E	HIS170	metal ligand

site_id	MCSA6
Number of Residues	4
Details	M-CSA 239

Chain	Residue	Details
F	ARG38	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	HIS42	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	ASN70	electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity
F	HIS170	metal ligand

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