Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1SOF

Crystal structure of the azotobacter vinelandii bacterioferritin at 2.6 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004322	molecular_function	ferroxidase activity
A	0005506	molecular_function	iron ion binding
A	0005829	cellular_component	cytosol
A	0006811	biological_process	monoatomic ion transport
A	0006826	biological_process	iron ion transport
A	0006879	biological_process	intracellular iron ion homeostasis
A	0008199	molecular_function	ferric iron binding
A	0016491	molecular_function	oxidoreductase activity
A	0020037	molecular_function	heme binding
A	0046872	molecular_function	metal ion binding
A	0140315	molecular_function	iron ion sequestering activity
B	0004322	molecular_function	ferroxidase activity
B	0005506	molecular_function	iron ion binding
B	0005829	cellular_component	cytosol
B	0006811	biological_process	monoatomic ion transport
B	0006826	biological_process	iron ion transport
B	0006879	biological_process	intracellular iron ion homeostasis
B	0008199	molecular_function	ferric iron binding
B	0016491	molecular_function	oxidoreductase activity
B	0020037	molecular_function	heme binding
B	0046872	molecular_function	metal ion binding
B	0140315	molecular_function	iron ion sequestering activity
C	0004322	molecular_function	ferroxidase activity
C	0005506	molecular_function	iron ion binding
C	0005829	cellular_component	cytosol
C	0006811	biological_process	monoatomic ion transport
C	0006826	biological_process	iron ion transport
C	0006879	biological_process	intracellular iron ion homeostasis
C	0008199	molecular_function	ferric iron binding
C	0016491	molecular_function	oxidoreductase activity
C	0020037	molecular_function	heme binding
C	0046872	molecular_function	metal ion binding
C	0140315	molecular_function	iron ion sequestering activity
D	0004322	molecular_function	ferroxidase activity
D	0005506	molecular_function	iron ion binding
D	0005829	cellular_component	cytosol
D	0006811	biological_process	monoatomic ion transport
D	0006826	biological_process	iron ion transport
D	0006879	biological_process	intracellular iron ion homeostasis
D	0008199	molecular_function	ferric iron binding
D	0016491	molecular_function	oxidoreductase activity
D	0020037	molecular_function	heme binding
D	0046872	molecular_function	metal ion binding
D	0140315	molecular_function	iron ion sequestering activity
E	0004322	molecular_function	ferroxidase activity
E	0005506	molecular_function	iron ion binding
E	0005829	cellular_component	cytosol
E	0006811	biological_process	monoatomic ion transport
E	0006826	biological_process	iron ion transport
E	0006879	biological_process	intracellular iron ion homeostasis
E	0008199	molecular_function	ferric iron binding
E	0016491	molecular_function	oxidoreductase activity
E	0020037	molecular_function	heme binding
E	0046872	molecular_function	metal ion binding
E	0140315	molecular_function	iron ion sequestering activity
F	0004322	molecular_function	ferroxidase activity
F	0005506	molecular_function	iron ion binding
F	0005829	cellular_component	cytosol
F	0006811	biological_process	monoatomic ion transport
F	0006826	biological_process	iron ion transport
F	0006879	biological_process	intracellular iron ion homeostasis
F	0008199	molecular_function	ferric iron binding
F	0016491	molecular_function	oxidoreductase activity
F	0020037	molecular_function	heme binding
F	0046872	molecular_function	metal ion binding
F	0140315	molecular_function	iron ion sequestering activity
G	0004322	molecular_function	ferroxidase activity
G	0005506	molecular_function	iron ion binding
G	0005829	cellular_component	cytosol
G	0006811	biological_process	monoatomic ion transport
G	0006826	biological_process	iron ion transport
G	0006879	biological_process	intracellular iron ion homeostasis
G	0008199	molecular_function	ferric iron binding
G	0016491	molecular_function	oxidoreductase activity
G	0020037	molecular_function	heme binding
G	0046872	molecular_function	metal ion binding
G	0140315	molecular_function	iron ion sequestering activity
H	0004322	molecular_function	ferroxidase activity
H	0005506	molecular_function	iron ion binding
H	0005829	cellular_component	cytosol
H	0006811	biological_process	monoatomic ion transport
H	0006826	biological_process	iron ion transport
H	0006879	biological_process	intracellular iron ion homeostasis
H	0008199	molecular_function	ferric iron binding
H	0016491	molecular_function	oxidoreductase activity
H	0020037	molecular_function	heme binding
H	0046872	molecular_function	metal ion binding
H	0140315	molecular_function	iron ion sequestering activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 A 202

Chain	Residue
A	GLU18
A	GLU51
A	HIS54
A	GLU127

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 B 202

Chain	Residue
B	GLU18
B	GLU51
B	HIS54
B	GLU127

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 C 202

Chain	Residue
C	GLU51
C	HIS54
C	ILE123
C	GLU127
C	GLU18

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 D 202

Chain	Residue
D	GLU18
D	GLU51
D	HIS54
D	GLU127

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 E 202

Chain	Residue
E	GLU18
E	GLU51
E	HIS54
E	GLU127

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 F 202

Chain	Residue
F	GLU18
F	GLU51
F	HIS54
F	GLU127

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 G 202

Chain	Residue
G	GLU18
G	GLU51
G	HIS54
G	GLU127

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 H 202

Chain	Residue
H	GLU18
H	GLU51
H	HIS54
H	GLU127

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 A 201

Chain	Residue
A	GLU51
A	GLU94
A	GLU127
A	HIS130
A	HOH421

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 B 201

Chain	Residue
B	GLU51
B	GLU94
B	GLU127
B	HOH1203
B	HOH1204

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 C 201

Chain	Residue
C	GLU51
C	GLU94
C	GLU127
C	HIS130

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE2 D 201

Chain	Residue
D	GLU51
D	GLU94
D	GLU127
D	HIS130
D	HOH512
D	HOH514

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 E 201

Chain	Residue
E	GLU51
E	GLU94
E	GLU127
E	HIS130
E	HOH3208

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 F 201

Chain	Residue
F	GLU51
F	GLU94
F	GLU127
F	HOH318

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 G 201

Chain	Residue
G	GLU51
G	GLU94
G	GLU127
G	HOH4213
G	HOH4229

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE2 H 201

Chain	Residue
H	GLU51
H	GLU94
H	GLU127
H	HIS130
H	HOH312
H	HOH330

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 501

Chain	Residue
D	GLU81
D	GLU85
D	HOH524
H	GLU85

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG G 502

Chain	Residue
C	GLU85
G	GLU81
G	GLU85
G	HOH4233

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 301

Chain	Residue
A	ASP132
A	GLU135
A	HOH409
A	HOH411
A	HOH419
A	HOH423

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 302

Chain	Residue
B	HOH1217
B	HOH1218
B	HOH1220
D	ASP34

site_id	CC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 303

Chain	Residue
C	HOH2203
C	HOH2229
E	ASP34

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 304

Chain	Residue
D	HOH507
D	HOH516
D	HOH523
D	HOH528

site_id	CC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 305

Chain	Residue
B	HOH1201
E	HOH3220
B	ASP34

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG F 306

Chain	Residue
A	HOH424
B	HOH1216
F	HOH316

site_id	CC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 307

Chain	Residue
F	ASP34
F	HOH308
G	ASP132
G	HOH4204
G	HOH4214

site_id	CC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG H 308

Chain	Residue
G	HOH4206
G	HOH4210
G	HOH4216
G	HOH4226
G	HOH4232
H	HOH322

site_id	CC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BA D 401

Chain	Residue
B	ASN148
B	GLN151
C	ASN148
C	GLN151
D	ASN148
D	GLN151
E	ASN148
E	GLN151

site_id	DC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BA A 402

Chain	Residue
A	ASN148
A	GLN151
F	ASN148
F	GLN151
G	ASN148
G	GLN151
H	ASN148
H	GLN151

site_id	DC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM B 1200

Chain	Residue
A	ASN23
A	PHE26
A	TYR45
A	ILE49
A	MET52
A	LYS53
A	ALA55
A	ASP56
B	LEU19
B	ILE22
B	ASN23
B	PHE26
B	TYR45
B	MET52

site_id	DC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HEM C 2200

Chain	Residue
C	ASN23
C	PHE26
C	TYR45
C	MET52
C	LYS53
C	ASP56
D	ASN23
D	PHE26
D	TYR45
D	MET52
D	LYS53

site_id	DC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE HEM E 3200

Chain	Residue
E	ASN23
E	PHE26
E	TYR45
E	MET52
E	LYS53
E	ILE59
F	PHE26
F	TYR45
F	MET52
F	LYS53

site_id	DC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE HEM G 4200

Chain	Residue
G	ASN23
G	PHE26
G	TYR45
G	MET52
G	ALA55
H	PHE26
H	TYR45
H	MET52
H	LYS53

Functional Information from PROSITE/UniProt

site_id	PS00549
Number of Residues	19
Details	BACTERIOFERRITIN Bacterioferritin signature. MkGdkiVIqhLnkiLgneL

Chain	Residue	Details
A	MET1-LEU19

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1152
Details	Domain: {"description":"Ferritin-like diiron","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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