Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1GGJ

CRYSTAL STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI, ASN201ALA VARIANT.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004096	molecular_function	catalase activity
A	0004601	molecular_function	peroxidase activity
A	0005506	molecular_function	iron ion binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006972	biological_process	hyperosmotic response
A	0006974	biological_process	DNA damage response
A	0006979	biological_process	response to oxidative stress
A	0020037	molecular_function	heme binding
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0042802	molecular_function	identical protein binding
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	0005506	molecular_function	iron ion binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006972	biological_process	hyperosmotic response
B	0006974	biological_process	DNA damage response
B	0006979	biological_process	response to oxidative stress
B	0020037	molecular_function	heme binding
B	0042744	biological_process	hydrogen peroxide catabolic process
B	0042802	molecular_function	identical protein binding
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	0005506	molecular_function	iron ion binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006972	biological_process	hyperosmotic response
C	0006974	biological_process	DNA damage response
C	0006979	biological_process	response to oxidative stress
C	0020037	molecular_function	heme binding
C	0042744	biological_process	hydrogen peroxide catabolic process
C	0042802	molecular_function	identical protein binding
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	0005506	molecular_function	iron ion binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006972	biological_process	hyperosmotic response
D	0006974	biological_process	DNA damage response
D	0006979	biological_process	response to oxidative stress
D	0020037	molecular_function	heme binding
D	0042744	biological_process	hydrogen peroxide catabolic process
D	0042802	molecular_function	identical protein binding
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	23
Details	BINDING SITE FOR RESIDUE HDD A 760

Chain	Residue
A	ARG125
A	ILE274
A	HIS275
A	PHE391
A	LEU407
A	ARG411
A	SER414
A	TYR415
A	THR418
A	GLN419
A	HOH784
A	VAL127
A	HOH831
A	HOH859
A	HOH1423
D	ASP118
A	HIS128
A	ARG165
A	GLY184
A	VAL199
A	GLY200
A	PHE206
A	PHE214

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HDD B 760

Chain	Residue
B	ARG125
B	VAL127
B	HIS128
B	ARG165
B	GLY184
B	VAL199
B	GLY200
B	PHE214
B	ILE274
B	HIS275
B	PHE391
B	LEU407
B	ARG411
B	SER414
B	TYR415
B	THR418
B	GLN419
B	HOH829
B	HOH875
B	HOH1414
C	ASP118

site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HDD C 760

Chain	Residue
C	ARG125
C	HIS128
C	ARG165
C	VAL199
C	GLY200
C	PHE206
C	PHE214
C	ILE274
C	HIS275
C	PHE391
C	LEU407
C	ARG411
C	SER414
C	TYR415
C	THR418
C	GLN419
C	HOH882
C	HOH930
C	HOH959
C	HOH1418

site_id	AC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HDD D 760

Chain	Residue
D	ARG125
D	HIS128
D	ARG165
D	GLY184
D	PHE185
D	VAL199
D	GLY200
D	PHE206
D	PHE214
D	ILE274
D	HIS275
D	PHE391
D	LEU407
D	ARG411
D	SER414
D	TYR415
D	THR418
D	GLN419
D	HOH923
D	HOH970

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ARG411-GLN419

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

Chain	Residue	Details
A	PHE117-ALA133

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: ACT_SITE => ECO:0000255\|PROSITE-ProRule:PRU10013

Chain	Residue	Details
A	HIS128
A	ALA201
B	HIS128
B	ALA201
C	HIS128
C	ALA201
D	HIS128
D	ALA201

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: axial binding residue

Chain	Residue	Details
A	TYR415
B	TYR415
C	TYR415
D	TYR415

site_id	SWS_FT_FI3
Number of Residues	8
Details	CROSSLNK: 3'-histidyl-3-tyrosine (His-Tyr)

Chain	Residue	Details
A	HIS392
A	TYR415
B	HIS392
B	TYR415
C	HIS392
C	TYR415
D	HIS392
D	TYR415

Catalytic Information from CSA

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

Chain	Residue	Details
A	ALA201
A	SER167
A	HIS128

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

Chain	Residue	Details
B	ALA201
B	SER167
B	HIS128

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

Chain	Residue	Details
C	ALA201
C	SER167
C	HIS128

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

Chain	Residue	Details
D	ALA201
D	SER167
D	HIS128

site_id	MCSA1
Number of Residues	3
Details	M-CSA 573

Chain	Residue	Details
A	HIS128	proton shuttle (general acid/base)
A	ALA201	electrostatic stabiliser
A	HIS392	proton shuttle (general acid/base)

site_id	MCSA2
Number of Residues	3
Details	M-CSA 573

Chain	Residue	Details
B	HIS128	proton shuttle (general acid/base)
B	ALA201	electrostatic stabiliser
B	HIS392	proton shuttle (general acid/base)

site_id	MCSA3
Number of Residues	3
Details	M-CSA 573

Chain	Residue	Details
C	HIS128	proton shuttle (general acid/base)
C	ALA201	electrostatic stabiliser
C	HIS392	proton shuttle (general acid/base)

site_id	MCSA4
Number of Residues	3
Details	M-CSA 573

Chain	Residue	Details
D	HIS128	proton shuttle (general acid/base)
D	ALA201	electrostatic stabiliser
D	HIS392	proton shuttle (general acid/base)

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