1GGK

CRYSTAL STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI, ASN201HIS 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	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 760

Chain	Residue
A	ARG125
A	ILE274
A	HIS275
A	PHE391
A	LEU407
A	ARG411
A	SER414
A	TYR415
A	THR418
A	GLN419
A	ARG422
A	ILE126
A	HOH783
A	HOH827
A	HOH854
A	HOH1067
A	VAL127
A	HIS128
A	ARG165
A	VAL199
A	GLY200
A	HIS201
A	PHE214

---

site_id	AC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM B 760

Chain	Residue
B	ARG125
B	VAL127
B	HIS128
B	ARG165
B	VAL199
B	GLY200
B	HIS201
B	PHE206
B	PHE214
B	HIS275
B	PHE391
B	LEU407
B	ARG411
B	SER414
B	TYR415
B	THR418
B	GLN419
B	ARG422
B	HOH812
B	HOH857
B	HOH886
B	HOH1082
C	ASP118

---

site_id	AC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM C 760

Chain	Residue
B	ASP118
C	ARG125
C	ILE126
C	HIS128
C	ARG165
C	VAL199
C	GLY200
C	HIS201
C	PHE214
C	HIS275
C	PHE391
C	LEU407
C	ARG411
C	SER414
C	TYR415
C	GLN419
C	ARG422
C	HOH800
C	HOH847
C	HOH889
C	HOH911

---

site_id	AC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM D 760

Chain	Residue
A	ASP118
D	ARG125
D	ILE126
D	HIS128
D	ARG165
D	GLY184
D	VAL199
D	GLY200
D	HIS201
D	PHE214
D	HIS275
D	PHE391
D	LEU407
D	ARG411
D	SER414
D	TYR415
D	THR418
D	GLN419
D	ARG422
D	HOH872
D	HOH915
D	HOH943

---

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	HIS201
B	HIS128
B	HIS201
C	HIS128
C	HIS201
D	HIS128
D	HIS201

---

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	HIS201	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	HIS201	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	HIS201	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	HIS201	electrostatic stabiliser
D	HIS392	proton shuttle (general acid/base)

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