Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1SI8

Crystal structure of E. faecalis 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	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	9
Details	BINDING SITE FOR RESIDUE SO4 A 2001

Chain	Residue
A	GLY15
A	ASP16
A	HIS35
A	HOH2033
A	HOH2073
A	HOH2078
A	HOH2117
A	HOH2251
D	HOH2075

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 B 2002

Chain	Residue
B	VAL14
B	GLY15
B	ASP16
B	HIS35
B	HOH2016
B	HOH2092
B	HOH2128
B	HOH2129
C	HOH2081
D	HOH2182

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 C 2003

Chain	Residue
B	HOH2117
C	GLY15
C	ASP16
C	HIS35
C	HOH2232
C	HOH2290
C	HOH2301
C	HOH2322

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 D 2004

Chain	Residue
A	HOH2045
D	VAL14
D	GLY15
D	ASP16
D	HIS35
D	HOH2245
D	HOH2290
D	HOH2308
D	HOH2313
D	HOH2347

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 2005

Chain	Residue
A	ARG182
A	HIS192
A	LYS216

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 2006

Chain	Residue
B	ARG182
B	HIS192
B	LYS216

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 2007

Chain	Residue
C	ARG182
C	HIS192
C	LYS216
C	HOH2316

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 2008

Chain	Residue
D	ARG182
D	HIS192
D	LYS216

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 2009

Chain	Residue
A	ARG45
B	ARG45
D	HOH2114

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL C 2010

Chain	Residue
A	HOH2150
B	HOH2255
C	ARG45
D	ARG45

site_id	BC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE HEM A 501

Chain	Residue
A	ARG51
A	VAL52
A	VAL53
A	HIS54
A	ARG91
A	GLY110
A	PHE111
A	VAL125
A	GLY126
A	ASN127
A	ALA137
A	PHE140
A	SER196
A	PHE313
A	LEU329
A	ARG333
A	TYR337
A	ALA340
A	HIS341
A	ARG344
A	HOH2023
A	HOH2038
A	HOH2124
A	HOH2179
D	ASN44

site_id	BC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEM B 501

Chain	Residue
B	HIS341
B	ARG344
B	HOH2014
B	HOH2075
B	HOH2096
B	HOH2166
C	ASN44
B	ARG51
B	VAL52
B	VAL53
B	HIS54
B	ARG91
B	GLY110
B	PHE111
B	VAL125
B	GLY126
B	ASN127
B	ALA137
B	PHE140
B	SER196
B	PHE313
B	LEU329
B	ARG333
B	TYR337

site_id	BC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEM C 501

Chain	Residue
B	ASN44
C	ARG51
C	VAL52
C	VAL53
C	HIS54
C	ARG91
C	GLY110
C	PHE111
C	VAL125
C	GLY126
C	ASN127
C	ALA137
C	PHE140
C	SER196
C	PHE313
C	LEU329
C	ARG333
C	TYR337
C	HIS341
C	ARG344
C	HOH2014
C	HOH2017
C	HOH2047
C	HOH2110

site_id	BC5
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEM D 501

Chain	Residue
A	ASN44
D	ARG51
D	VAL52
D	VAL53
D	HIS54
D	ARG91
D	GLY110
D	PHE111
D	VAL125
D	GLY126
D	ASN127
D	ALA137
D	PHE140
D	SER196
D	PHE313
D	LEU329
D	ARG333
D	TYR337
D	HIS341
D	ARG344
D	HOH2015
D	HOH2021
D	HOH2024
D	HOH2328

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ARG333-HIS341

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

Chain	Residue	Details
A	PHE43-GLY59

Catalytic Information from CSA

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

Chain	Residue	Details
A	HIS54
A	ASN127
A	SER93

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

Chain	Residue	Details
B	HIS54
B	ASN127
B	SER93

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

Chain	Residue	Details
C	HIS54
C	ASN127
C	SER93

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

Chain	Residue	Details
D	HIS54
D	ASN127
D	SER93

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