Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QF7

STRUCTURE OF THE MUTANT HIS392GLN OF CATALASE HPII FROM E. COLI

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	0016491	molecular_function	oxidoreductase activity
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	0016491	molecular_function	oxidoreductase activity
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	0016491	molecular_function	oxidoreductase activity
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	0016491	molecular_function	oxidoreductase activity
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 HEM A 754

Chain	Residue
A	ARG125
A	ILE126
A	VAL127
A	HIS128
A	ARG165
A	GLY184
A	VAL199
A	GLY200
A	ASN201
A	PHE214
A	ILE274
A	HIS275
A	PHE391
A	LEU407
A	ARG411
A	SER414
A	TYR415
A	THR418
A	GLN419
A	ARG422
A	HOH775
A	HOH824
A	HOH856

site_id	AC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE HEM B 754

Chain	Residue
B	ARG125
B	ILE126
B	VAL127
B	HIS128
B	ARG165
B	GLY184
B	VAL199
B	GLY200
B	ASN201
B	PHE206
B	PHE214
B	ILE274
B	HIS275
B	PHE391
B	LEU407
B	ARG411
B	SER414
B	TYR415
B	THR418
B	GLN419
B	ARG422
B	HOH782
B	HOH831
B	HOH864
B	HOH1377
C	ASP118

site_id	AC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM C 754

Chain	Residue
C	ARG125
C	ILE126
C	VAL127
C	HIS128
C	ARG165
C	GLY184
C	VAL199
C	GLY200
C	ASN201
C	PHE214
C	HIS275
C	PHE391
C	LEU407
C	ARG411
C	SER414
C	TYR415
C	THR418
C	GLN419
C	ARG422
C	HOH816
C	HOH864
C	HOH899

site_id	AC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEM D 754

Chain	Residue
D	SER414
D	TYR415
D	THR418
D	GLN419
D	ARG422
D	HOH829
D	HOH878
D	HOH910
A	ASP118
D	ARG125
D	ILE126
D	VAL127
D	HIS128
D	ARG165
D	GLY184
D	VAL199
D	GLY200
D	ASN201
D	PHE214
D	ILE274
D	HIS275
D	PHE391
D	LEU407
D	ARG411

site_id	CAA
Number of Residues	3
Details	ESSENTIAL CATALYTIC RESIDUES.

Chain	Residue
A	HIS128
A	ASN201
A	TYR415

site_id	CAB
Number of Residues	3
Details	ESSENTIAL CATALYTIC RESIDUES.

Chain	Residue
B	HIS128
B	ASN201
B	TYR415

site_id	CAC
Number of Residues	3
Details	ESSENTIAL CATALYTIC RESIDUES.

Chain	Residue
C	HIS128
C	ASN201
C	TYR415

site_id	CAD
Number of Residues	3
Details	ESSENTIAL CATALYTIC RESIDUES.

Chain	Residue
D	HIS128
D	ASN201
D	TYR415

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	ASN201
B	HIS128
B	ASN201
C	HIS128
C	ASN201
D	HIS128
D	ASN201

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	GLN392
A	TYR415
B	GLN392
B	TYR415
C	GLN392
C	TYR415
D	GLN392
D	TYR415

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 573

Chain	Residue	Details
A	HIS128	proton shuttle (general acid/base)
A	ASN201	electrostatic stabiliser
A	GLN392	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	ASN201	electrostatic stabiliser
B	GLN392	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	ASN201	electrostatic stabiliser
C	GLN392	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	ASN201	electrostatic stabiliser
D	GLN392	proton shuttle (general acid/base)

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