Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2HTN

E. coli bacterioferritin in its as-isolated form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004322	molecular_function	ferroxidase activity
A	0005506	molecular_function	iron ion binding
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0006826	biological_process	iron ion transport
A	0006879	biological_process	intracellular iron ion homeostasis
A	0006880	biological_process	intracellular sequestering of iron ion
A	0008199	molecular_function	ferric iron binding
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0020037	molecular_function	heme binding
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
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	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0006826	biological_process	iron ion transport
B	0006879	biological_process	intracellular iron ion homeostasis
B	0006880	biological_process	intracellular sequestering of iron ion
B	0008199	molecular_function	ferric iron binding
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0020037	molecular_function	heme binding
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
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	0005515	molecular_function	protein binding
C	0005829	cellular_component	cytosol
C	0006826	biological_process	iron ion transport
C	0006879	biological_process	intracellular iron ion homeostasis
C	0006880	biological_process	intracellular sequestering of iron ion
C	0008199	molecular_function	ferric iron binding
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0020037	molecular_function	heme binding
C	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
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	0005515	molecular_function	protein binding
D	0005829	cellular_component	cytosol
D	0006826	biological_process	iron ion transport
D	0006879	biological_process	intracellular iron ion homeostasis
D	0006880	biological_process	intracellular sequestering of iron ion
D	0008199	molecular_function	ferric iron binding
D	0016020	cellular_component	membrane
D	0016491	molecular_function	oxidoreductase activity
D	0020037	molecular_function	heme binding
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity
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	0005515	molecular_function	protein binding
E	0005829	cellular_component	cytosol
E	0006826	biological_process	iron ion transport
E	0006879	biological_process	intracellular iron ion homeostasis
E	0006880	biological_process	intracellular sequestering of iron ion
E	0008199	molecular_function	ferric iron binding
E	0016020	cellular_component	membrane
E	0016491	molecular_function	oxidoreductase activity
E	0020037	molecular_function	heme binding
E	0042802	molecular_function	identical protein binding
E	0042803	molecular_function	protein homodimerization activity
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	0005515	molecular_function	protein binding
F	0005829	cellular_component	cytosol
F	0006826	biological_process	iron ion transport
F	0006879	biological_process	intracellular iron ion homeostasis
F	0006880	biological_process	intracellular sequestering of iron ion
F	0008199	molecular_function	ferric iron binding
F	0016020	cellular_component	membrane
F	0016491	molecular_function	oxidoreductase activity
F	0020037	molecular_function	heme binding
F	0042802	molecular_function	identical protein binding
F	0042803	molecular_function	protein homodimerization activity
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	0005515	molecular_function	protein binding
G	0005829	cellular_component	cytosol
G	0006826	biological_process	iron ion transport
G	0006879	biological_process	intracellular iron ion homeostasis
G	0006880	biological_process	intracellular sequestering of iron ion
G	0008199	molecular_function	ferric iron binding
G	0016020	cellular_component	membrane
G	0016491	molecular_function	oxidoreductase activity
G	0020037	molecular_function	heme binding
G	0042802	molecular_function	identical protein binding
G	0042803	molecular_function	protein homodimerization activity
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	0005515	molecular_function	protein binding
H	0005829	cellular_component	cytosol
H	0006826	biological_process	iron ion transport
H	0006879	biological_process	intracellular iron ion homeostasis
H	0006880	biological_process	intracellular sequestering of iron ion
H	0008199	molecular_function	ferric iron binding
H	0016020	cellular_component	membrane
H	0016491	molecular_function	oxidoreductase activity
H	0020037	molecular_function	heme binding
H	0042802	molecular_function	identical protein binding
H	0042803	molecular_function	protein homodimerization activity
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 FE A 301

Chain	Residue
A	GLU18
A	GLU51
A	HIS54
A	GLU127

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE A 302

Chain	Residue
A	GLU51
A	GLU94
A	GLU127
A	HIS130

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE B 301

Chain	Residue
B	GLU51
B	HIS54
B	GLU127
B	FE302
B	GLU18

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE B 302

Chain	Residue
B	GLU51
B	GLU94
B	GLU127
B	HIS130
B	FE301

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE C 301

Chain	Residue
C	GLU18
C	GLU51
C	HIS54
C	GLU127
C	FE302

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE C 302

Chain	Residue
C	GLU51
C	GLU94
C	GLU127
C	HIS130
C	FE301

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE D 301

Chain	Residue
D	GLU18
D	GLU51
D	HIS54
D	GLU127

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE D 302

Chain	Residue
D	GLU51
D	GLU94
D	GLU127
D	HIS130

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE E 301

Chain	Residue
E	GLU18
E	GLU51
E	HIS54
E	GLU127

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE E 302

Chain	Residue
E	GLU51
E	GLU94
E	GLU127
E	HIS130
E	HOH311

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE F 301

Chain	Residue
F	GLU18
F	GLU51
F	HIS54
F	GLU127

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE F 302

Chain	Residue
F	GLU51
F	GLU94
F	GLU127
F	HIS130

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE G 301

Chain	Residue
G	GLU18
G	GLU51
G	HIS54
G	GLU127

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE G 302

Chain	Residue
G	GLU51
G	GLU94
G	GLU127
G	HIS130

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE H 301

Chain	Residue
H	GLU18
H	GLU51
H	HIS54
H	GLU127

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE H 302

Chain	Residue
H	GLU51
H	GLU94
H	GLU127
H	HIS130

site_id	BC8
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM A 200

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

site_id	BC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM C 200

Chain	Residue
D	MET52
D	LYS53
D	ALA55
C	ILE22
C	ASN23
C	PHE26
C	TYR45
C	ILE49
C	MET52
C	LYS53
C	ALA55
C	ASP56
D	ASN23
D	PHE26
D	TYR45

site_id	CC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM E 200

Chain	Residue
E	ILE22
E	ASN23
E	PHE26
E	TYR45
E	MET52
E	LYS53
E	ALA55
F	ILE22
F	ASN23
F	PHE26
F	TYR45
F	ILE49
F	MET52
F	LYS53
F	ALA55

site_id	CC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM G 200

Chain	Residue
G	ILE22
G	ASN23
G	PHE26
G	TYR45
G	ILE49
G	MET52
G	LYS53
G	ALA55
H	ILE22
H	ASN23
H	PHE26
H	TYR45
H	MET52
H	ALA55

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	MET1-LEU19

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	64
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00085, ECO:0000269\|PubMed:17077480

Chain	Residue	Details
A	GLU18
B	HIS46
B	ASP50
B	GLU51
B	HIS54
B	GLU94
B	GLU127
B	HIS130
C	GLU18
C	HIS46
C	ASP50
A	HIS46
C	GLU51
C	HIS54
C	GLU94
C	GLU127
C	HIS130
D	GLU18
D	HIS46
D	ASP50
D	GLU51
D	HIS54
A	ASP50
D	GLU94
D	GLU127
D	HIS130
E	GLU18
E	HIS46
E	ASP50
E	GLU51
E	HIS54
E	GLU94
E	GLU127
A	GLU51
E	HIS130
F	GLU18
F	HIS46
F	ASP50
F	GLU51
F	HIS54
F	GLU94
F	GLU127
F	HIS130
G	GLU18
A	HIS54
G	HIS46
G	ASP50
G	GLU51
G	HIS54
G	GLU94
G	GLU127
G	HIS130
H	GLU18
H	HIS46
H	ASP50
A	GLU94
H	GLU51
H	HIS54
H	GLU94
H	GLU127
H	HIS130
A	GLU127
A	HIS130
B	GLU18

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: axial binding residue => ECO:0000255\|PROSITE-ProRule:PRU00085, ECO:0000269\|PubMed:17077480

Chain	Residue	Details
A	MET52
B	MET52
C	MET52
D	MET52
E	MET52
F	MET52
G	MET52
H	MET52

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