Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3RGS

Structural and kinetic analysis of the beef liver catalase with the ammonia as a ligand

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	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	0098869	biological_process	cellular oxidant detoxification
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	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	0098869	biological_process	cellular oxidant detoxification
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	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	0098869	biological_process	cellular oxidant detoxification
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	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	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	27
Details	BINDING SITE FOR RESIDUE HEM A 1

Chain	Residue
A	ARG71
A	ALA157
A	PHE160
A	GLY215
A	SER216
A	LEU298
A	PHE333
A	MET349
A	ARG353
A	TYR357
A	THR360
A	VAL72
A	HIS361
A	ARG364
A	NH3502
A	HOH511
A	HOH542
A	HOH621
D	MET60
D	ASP64
A	VAL73
A	HIS74
A	ARG111
A	GLY130
A	VAL145
A	GLY146
A	ASN147

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NH3 A 502

Chain	Residue
A	HEM1
A	HIS74
A	PHE160
A	HOH566

site_id	AC3
Number of Residues	29
Details	BINDING SITE FOR RESIDUE HEM B 1

Chain	Residue
B	ARG71
B	VAL72
B	VAL73
B	HIS74
B	ARG111
B	GLY130
B	VAL145
B	GLY146
B	ASN147
B	ALA157
B	PHE160
B	GLY215
B	SER216
B	LEU298
B	PHE333
B	MET349
B	ARG353
B	TYR357
B	THR360
B	HIS361
B	ARG364
B	NH3502
B	HOH552
B	HOH669
B	HOH754
B	HOH789
B	HOH2260
C	MET60
C	ASP64

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NH3 B 502

Chain	Residue
B	HEM1
B	HIS74
B	PHE160
B	HOH1295

site_id	AC5
Number of Residues	28
Details	BINDING SITE FOR RESIDUE HEM C 1

Chain	Residue
B	MET60
B	ASP64
C	ARG71
C	VAL72
C	HIS74
C	ARG111
C	GLY130
C	VAL145
C	GLY146
C	ASN147
C	ALA157
C	PHE160
C	GLY215
C	SER216
C	LEU298
C	PHE333
C	MET349
C	ARG353
C	ALA356
C	TYR357
C	THR360
C	HIS361
C	ARG364
C	NH3502
C	HOH504
C	HOH546
C	HOH566
C	HOH2159

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NH3 C 502

Chain	Residue
C	HEM1
C	HIS74
C	PHE160
C	HOH1440

site_id	AC7
Number of Residues	27
Details	BINDING SITE FOR RESIDUE HEM D 1

Chain	Residue
D	VAL72
D	VAL73
D	HIS74
D	ARG111
D	GLY130
D	VAL145
D	GLY146
D	ASN147
D	ALA157
D	PHE160
D	GLY215
D	SER216
D	LEU298
D	PHE333
D	MET349
D	ARG353
D	TYR357
D	THR360
D	HIS361
D	ARG364
D	NH3502
D	HOH522
D	HOH527
D	HOH541
A	MET60
A	ASP64
D	ARG71

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NH3 D 502

Chain	Residue
D	HEM1
D	VAL73
D	HIS74
D	PHE160
D	HOH778

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	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10013","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7328661","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10013","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10417406","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BLC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P04040","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10417406","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BLC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04040","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P24270","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P24270","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P24270","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P24270","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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