4CAB

The refined structure of catalase DR1998 from Deinococcus radiodurans at 2.6 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004096	molecular_function	catalase activity
A	0004601	molecular_function	peroxidase activity
A	0005737	cellular_component	cytoplasm
A	0006979	biological_process	response to oxidative stress
A	0016491	molecular_function	oxidoreductase activity
A	0020037	molecular_function	heme binding
A	0042542	biological_process	response to hydrogen peroxide
A	0042744	biological_process	hydrogen peroxide catabolic process
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	0005737	cellular_component	cytoplasm
B	0006979	biological_process	response to oxidative stress
B	0016491	molecular_function	oxidoreductase activity
B	0020037	molecular_function	heme binding
B	0042542	biological_process	response to hydrogen peroxide
B	0042744	biological_process	hydrogen peroxide catabolic process
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	0005737	cellular_component	cytoplasm
C	0006979	biological_process	response to oxidative stress
C	0016491	molecular_function	oxidoreductase activity
C	0020037	molecular_function	heme binding
C	0042542	biological_process	response to hydrogen peroxide
C	0042744	biological_process	hydrogen peroxide catabolic process
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	0005737	cellular_component	cytoplasm
D	0006979	biological_process	response to oxidative stress
D	0016491	molecular_function	oxidoreductase activity
D	0020037	molecular_function	heme binding
D	0042542	biological_process	response to hydrogen peroxide
D	0042744	biological_process	hydrogen peroxide catabolic process
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	24
Details	BINDING SITE FOR RESIDUE HEM A 537

Chain	Residue
A	ARG78
A	PHE172
A	VAL228
A	ASN229
A	ASP310
A	PHE345
A	MET361
A	ARG365
A	SER368
A	TYR369
A	THR372
A	VAL79
A	GLN373
A	ARG376
A	HOH2023
B	LEU67
B	ASP71
A	VAL80
A	HIS81
A	ARG123
A	GLY142
A	VAL157
A	GLY158
A	ASN159

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CL A 1537

Chain	Residue
A	ARG36
A	HIS69
A	ARG374
A	PRO379
A	ASN380
A	LEU382
A	HOH2109

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 1538

Chain	Residue
A	LYS66
A	ASN396
A	HOH2002
A	HOH2116

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL A 1539

Chain	Residue
A	ARG487
B	LEU422
B	LEU423
D	GLU509
D	GLN512

---

site_id	AC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE HEM B 537

Chain	Residue
A	LEU67
A	ASP71
B	ARG78
B	VAL79
B	VAL80
B	HIS81
B	ARG123
B	GLY142
B	VAL157
B	GLY158
B	ASN159
B	PHE172
B	VAL228
B	ASN229
B	ASP310
B	PHE345
B	MET361
B	ARG365
B	SER368
B	TYR369
B	THR372
B	GLN373
B	ARG376
B	HOH2025
B	HOH2086

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL B 1537

Chain	Residue
B	ARG36
B	HIS69
B	ARG374
B	PRO379
B	ASN380
B	LEU382

---

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL B 1538

Chain	Residue
B	ARG254

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B 1002

Chain	Residue
A	HOH2027
B	LYS66
B	ASN396
B	HOH2002

---

site_id	AC9
Number of Residues	25
Details	BINDING SITE FOR RESIDUE HEM C 537

Chain	Residue
C	HOH2038
C	HOH2123
C	LEU67
C	ASP71
C	ARG78
C	VAL79
C	VAL80
C	HIS81
C	ARG123
C	VAL157
C	GLY158
C	ASN159
C	ALA169
C	PHE172
C	VAL228
C	ASN229
C	ASP310
C	PHE345
C	MET361
C	ARG365
C	SER368
C	TYR369
C	THR372
C	GLN373
C	ARG376

---

site_id	BC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL C 1537

Chain	Residue
C	ARG439

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL C 1538

Chain	Residue
C	ARG374
C	PRO379
C	ASN380
C	TYR381
C	LEU382
D	ARG36

---

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL C 1002

Chain	Residue
C	LYS66
D	ASN396

---

site_id	BC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM D 537

Chain	Residue
D	LEU67
D	ASP71
D	ARG78
D	VAL79
D	VAL80
D	HIS81
D	ARG123
D	VAL157
D	GLY158
D	ASN159
D	PHE172
D	VAL228
D	ASN229
D	PHE345
D	MET361
D	ARG365
D	SER368
D	TYR369
D	THR372
D	GLN373
D	ARG376
D	HOH2015
D	HOH2030

---

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL D 1537

Chain	Residue
C	ARG36
D	ARG374
D	PRO379
D	ASN380
D	LEU382

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ARG365-GLN373

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	164
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	44
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---