Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1YE9

Crystal structure of proteolytically truncated catalase HPII from E. coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004096	molecular_function	catalase activity
A	0006979	biological_process	response to oxidative stress
A	0020037	molecular_function	heme binding
B	0004096	molecular_function	catalase activity
B	0006979	biological_process	response to oxidative stress
B	0020037	molecular_function	heme binding
C	0004096	molecular_function	catalase activity
C	0006979	biological_process	response to oxidative stress
C	0020037	molecular_function	heme binding
D	0004096	molecular_function	catalase activity
D	0006979	biological_process	response to oxidative stress
D	0020037	molecular_function	heme binding
E	0004096	molecular_function	catalase activity
E	0006979	biological_process	response to oxidative stress
E	0020037	molecular_function	heme binding
F	0004096	molecular_function	catalase activity
F	0006979	biological_process	response to oxidative stress
F	0020037	molecular_function	heme binding
G	0004096	molecular_function	catalase activity
G	0006979	biological_process	response to oxidative stress
G	0020037	molecular_function	heme binding
H	0004096	molecular_function	catalase activity
H	0006979	biological_process	response to oxidative stress
H	0020037	molecular_function	heme binding
I	0004096	molecular_function	catalase activity
I	0006979	biological_process	response to oxidative stress
I	0020037	molecular_function	heme binding
J	0004096	molecular_function	catalase activity
J	0006979	biological_process	response to oxidative stress
J	0020037	molecular_function	heme binding
K	0004096	molecular_function	catalase activity
K	0006979	biological_process	response to oxidative stress
K	0020037	molecular_function	heme binding
L	0004096	molecular_function	catalase activity
L	0006979	biological_process	response to oxidative stress
L	0020037	molecular_function	heme binding
M	0004096	molecular_function	catalase activity
M	0006979	biological_process	response to oxidative stress
M	0020037	molecular_function	heme binding
N	0004096	molecular_function	catalase activity
N	0006979	biological_process	response to oxidative stress
N	0020037	molecular_function	heme binding
O	0004096	molecular_function	catalase activity
O	0006979	biological_process	response to oxidative stress
O	0020037	molecular_function	heme binding
P	0004096	molecular_function	catalase activity
P	0006979	biological_process	response to oxidative stress
P	0020037	molecular_function	heme binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HDD E 760

Chain	Residue
A	ARG125
A	PHE214
A	ILE274
A	HOH303
D	PHE117
E	HOH137
E	PHE391
E	LEU407
E	ARG411
E	SER414
E	TYR415
A	VAL127
E	GLN419
A	HIS128
A	ARG165
A	GLY184
A	VAL199
A	GLY200
A	ASN201
A	PHE206

site_id	AC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HDD F 760

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
F	PHE391
F	LEU407
F	ARG411
F	SER414
F	TYR415
F	THR418
F	GLN419
F	ARG422

site_id	AC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HDD G 760

Chain	Residue
B	PHE117
C	ARG125
C	ILE126
C	VAL127
C	HIS128
C	ARG165
C	GLY184
C	VAL199
C	GLY200
C	ASN201
C	PHE206
C	PHE214
C	ILE274
C	HIS275
G	PHE391
G	LEU407
G	ARG411
G	SER414
G	TYR415
G	THR418
G	GLN419

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HDD H 760

Chain	Residue
D	ARG125
D	ILE126
D	VAL127
D	HIS128
D	ARG165
D	GLY184
D	VAL199
D	GLY200
D	ASN201
D	PHE206
D	PHE214
H	PHE391
H	LEU407
H	ARG411
H	SER414
H	TYR415
H	THR418
H	GLN419
H	ARG422

site_id	AC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HDD M 760

Chain	Residue
I	ARG125
I	ILE126
I	VAL127
I	HIS128
I	ARG165
I	GLY184
I	VAL199
I	GLY200
I	ASN201
I	PHE214
I	HIS275
M	PHE391
M	LEU407
M	ARG411
M	SER414
M	TYR415
M	THR418
M	GLN419

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HDD N 760

Chain	Residue
J	VAL127
J	HIS128
J	ARG165
J	GLY184
J	VAL199
J	GLY200
J	ASN201
J	PHE206
J	PHE214
J	ILE274
K	PHE117
N	PHE391
N	LEU407
N	ARG411
N	SER414
N	TYR415
N	GLN419
J	ARG125

site_id	AC7
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HDD O 760

Chain	Residue
K	ARG125
K	VAL127
K	HIS128
K	ARG165
K	GLY184
K	VAL199
K	GLY200
K	ASN201
K	PHE206
K	PHE214
K	HIS275
O	PHE391
O	LEU407
O	ARG411
O	SER414
O	TYR415
O	THR418
O	GLN419
O	ARG422
O	HOH761

site_id	AC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HDD P 760

Chain	Residue
L	ARG125
L	ILE126
L	VAL127
L	HIS128
L	ARG165
L	GLY184
L	ALA186
L	VAL199
L	GLY200
L	ASN201
L	PHE206
L	PHE214
L	ILE274
P	PHE391
P	ARG411
P	SER414
P	TYR415
P	THR418
P	GLN419
P	ARG422

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE117-ALA133

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

Chain	Residue	Details
E	ARG411-GLN419

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10013","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	272
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	16
Details	Cross-link: {"description":"3'-histidyl-3-tyrosine (His-Tyr)"}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASN201
A	SER167
A	HIS128

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

Chain	Residue	Details
B	ASN201
B	SER167
B	HIS128

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

Chain	Residue	Details
C	ASN201
C	SER167
C	HIS128

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

Chain	Residue	Details
D	ASN201
D	SER167
D	HIS128

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1iph

Chain	Residue	Details
I	ASN201
I	SER167
I	HIS128

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1iph

Chain	Residue	Details
J	ASN201
J	SER167
J	HIS128

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1iph

Chain	Residue	Details
K	ASN201
K	SER167
K	HIS128

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1iph

Chain	Residue	Details
L	ASN201
L	SER167
L	HIS128

site_id	MCSA1
Number of Residues	1
Details	M-CSA 573

Chain	Residue	Details
B	LYS158	proton shuttle (general acid/base)
A	ASN201	electrostatic stabiliser

site_id	MCSA2
Number of Residues	1
Details	M-CSA 573

Chain	Residue	Details
D	LYS158	proton shuttle (general acid/base)
C	ASN201	electrostatic stabiliser

site_id	MCSA3
Number of Residues	1
Details	M-CSA 573

Chain	Residue	Details
F	HIS392	proton shuttle (general acid/base)
E	ARG435	electrostatic stabiliser

site_id	MCSA4
Number of Residues	1
Details	M-CSA 573

Chain	Residue	Details
H	HIS392	proton shuttle (general acid/base)
G	ARG435	electrostatic stabiliser

site_id	MCSA5
Number of Residues	1
Details	M-CSA 573

Chain	Residue	Details
J	LYS158	proton shuttle (general acid/base)
I	ASN201	electrostatic stabiliser

site_id	MCSA6
Number of Residues	1
Details	M-CSA 573

Chain	Residue	Details
L	LYS158	proton shuttle (general acid/base)
K	ASN201	electrostatic stabiliser

site_id	MCSA7
Number of Residues	1
Details	M-CSA 573

Chain	Residue	Details
N	HIS392	proton shuttle (general acid/base)
M	ARG435	electrostatic stabiliser

site_id	MCSA8
Number of Residues	1
Details	M-CSA 573

Chain	Residue	Details
P	HIS392	proton shuttle (general acid/base)
O	ARG435	electrostatic stabiliser

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