Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3P9P

Structure of I274V variant of E. coli KatE

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	25
Details	BINDING SITE FOR RESIDUE HEM A 754

Chain	Residue
A	ARG125
A	VAL274
A	HIS275
A	PHE391
A	LEU407
A	GLY410
A	ARG411
A	SER414
A	TYR415
A	THR418
A	GLN419
A	VAL127
A	ARG422
A	HOH795
A	HOH850
A	HOH880
A	HOH2309
D	ASP118
A	HIS128
A	ARG165
A	GLY184
A	VAL199
A	GLY200
A	ASN201
A	PHE214

site_id	AC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HDE A 761

Chain	Residue
A	ARG125
A	VAL127
A	HIS128
A	ARG165
A	VAL199
A	GLY200
A	ASN201
A	PHE206
A	ALA211
A	PHE214
A	GLY273
A	VAL274
A	PHE391
A	LEU407
A	ARG411
A	SER414
A	TYR415
A	THR418
A	GLN419
A	HOH795
A	HOH850
A	HOH2309

site_id	AC3
Number of Residues	25
Details	BINDING SITE FOR RESIDUE HEM A 755

Chain	Residue
A	ARG125
A	VAL127
A	HIS128
A	ARG165
A	GLY184
A	VAL199
A	GLY200
A	ASN201
A	ALA211
A	PHE214
A	GLY273
A	VAL274
A	HIS275
A	PHE391
A	LEU407
A	ARG411
A	SER414
A	TYR415
A	THR418
A	GLN419
A	ARG422
A	HOH795
A	HOH850
A	HOH880
A	HOH2309

site_id	AC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HDD A 760

Chain	Residue
A	ARG125
A	VAL127
A	HIS128
A	ARG165
A	GLY184
A	VAL199
A	GLY200
A	ASN201
A	PHE206
A	PHE214
A	VAL274
A	HIS275
A	PHE391
A	LEU407
A	ARG411
A	SER414
A	TYR415
A	THR418
A	GLN419
A	HOH795
A	HOH850
A	HOH880
A	HOH2309

site_id	AC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE HEM B 754

Chain	Residue
B	GLY184
B	VAL199
B	GLY200
B	ASN201
B	PHE206
B	PHE214
B	VAL274
B	HIS275
B	LEU407
B	GLY410
B	ARG411
B	SER414
B	TYR415
B	THR418
B	GLN419
B	ARG422
B	HOH845
B	HOH898
B	HOH927
B	HOH3444
C	ASP118
B	ARG125
B	VAL127
B	HIS128
B	ARG165

site_id	AC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HDE B 761

Chain	Residue
B	ARG125
B	VAL127
B	HIS128
B	ARG165
B	GLY184
B	VAL199
B	GLY200
B	ASN201
B	ALA211
B	PHE214
B	GLY273
B	VAL274
B	PHE391
B	LEU407
B	ARG411
B	SER414
B	TYR415
B	THR418
B	GLN419
B	HOH840
B	HOH845
B	HOH898
B	HOH3444

site_id	AC7
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEM B 755

Chain	Residue
B	ARG125
B	VAL127
B	HIS128
B	ARG165
B	GLY184
B	VAL199
B	GLY200
B	ASN201
B	ALA211
B	PHE214
B	VAL274
B	PHE391
B	LEU407
B	ARG411
B	SER414
B	TYR415
B	THR418
B	GLN419
B	ARG422
B	HOH845
B	HOH898
B	HOH927
B	HOH3444
C	ASP118

site_id	AC8
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	ASN201
B	PHE206
B	PHE214
B	HIS275
B	PHE391
B	LEU407
B	ARG411
B	SER414
B	TYR415
B	THR418
B	GLN419
B	HOH845
B	HOH898
B	HOH3444

site_id	AC9
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEM C 754

Chain	Residue
C	ARG125
C	VAL127
C	HIS128
C	ARG165
C	GLY184
C	VAL199
C	GLY200
C	ASN201
C	PHE206
C	PHE214
C	VAL274
C	HIS275
C	PHE391
C	LEU407
C	ARG411
C	SER414
C	TYR415
C	THR418
C	GLN419
C	ARG422
C	HOH871
C	HOH929
C	HOH964
C	HOH3362

site_id	BC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HDE C 761

Chain	Residue
C	ARG125
C	VAL127
C	HIS128
C	ARG165
C	VAL199
C	GLY200
C	ASN201
C	ALA211
C	PHE214
C	GLY273
C	VAL274
C	PHE391
C	LEU407
C	ARG411
C	SER414
C	TYR415
C	THR418
C	GLN419
C	HOH871
C	HOH929
C	HOH964
C	HOH1263
C	HOH3362

site_id	BC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM C 755

Chain	Residue
C	ARG125
C	VAL127
C	HIS128
C	ARG165
C	GLY184
C	VAL199
C	GLY200
C	ASN201
C	ALA211
C	PHE214
C	VAL274
C	PHE391
C	LEU407
C	ARG411
C	SER414
C	TYR415
C	THR418
C	GLN419
C	ARG422
C	HOH871
C	HOH929
C	HOH964
C	HOH3362

site_id	BC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HDD C 760

Chain	Residue
C	ARG125
C	VAL127
C	HIS128
C	ARG165
C	GLY184
C	VAL199
C	GLY200
C	ASN201
C	PHE206
C	PHE214
C	VAL274
C	HIS275
C	PHE391
C	LEU407
C	ARG411
C	SER414
C	TYR415
C	THR418
C	GLN419
C	HOH871
C	HOH929
C	HOH964
C	HOH3362

site_id	BC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEM D 754

Chain	Residue
A	ASP118
D	ARG125
D	VAL127
D	HIS128
D	ARG165
D	GLY184
D	VAL199
D	GLY200
D	ASN201
D	PHE206
D	PHE214
D	HIS275
D	PHE391
D	LEU407
D	GLY410
D	ARG411
D	SER414
D	TYR415
D	THR418
D	GLN419
D	ARG422
D	HOH1295
D	HOH1353
D	HOH1388

site_id	BC5
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HDE D 761

Chain	Residue
D	ARG125
D	VAL127
D	HIS128
D	ARG165
D	GLY184
D	VAL199
D	GLY200
D	ASN201
D	PHE206
D	ALA211
D	PHE214
D	GLY273
D	VAL274
D	PHE391
D	LEU407
D	ARG411
D	SER414
D	TYR415
D	THR418
D	GLN419
D	HOH1295
D	HOH1353

site_id	BC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM D 755

Chain	Residue
A	ASP118
D	ARG125
D	VAL127
D	HIS128
D	ARG165
D	GLY184
D	VAL199
D	GLY200
D	ASN201
D	ALA211
D	PHE214
D	VAL274
D	PHE391
D	LEU407
D	ARG411
D	SER414
D	TYR415
D	THR418
D	GLN419
D	ARG422
D	HOH1295
D	HOH1353
D	HOH1388

site_id	BC7
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HDD D 760

Chain	Residue
D	ARG125
D	VAL127
D	HIS128
D	ARG165
D	GLY184
D	VAL199
D	GLY200
D	ASN201
D	PHE206
D	PHE214
D	VAL274
D	HIS275
D	PHE391
D	LEU407
D	ARG411
D	SER414
D	TYR415
D	THR418
D	GLN419
D	HOH1295
D	HOH1353
D	HOH1388

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	HIS392
A	TYR415
B	HIS392
B	TYR415
C	HIS392
C	TYR415
D	HIS392
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	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	ASN201	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	ASN201	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	ASN201	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)