Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3UOF

Mycobacterium tuberculosis bacterioferritin, BfrA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004322	molecular_function	ferroxidase activity
A	0005506	molecular_function	iron ion binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006826	biological_process	iron ion transport
A	0006879	biological_process	intracellular iron ion homeostasis
A	0008199	molecular_function	ferric iron binding
A	0010039	biological_process	response to iron ion
A	0016491	molecular_function	oxidoreductase activity
A	0020037	molecular_function	heme binding
A	0046872	molecular_function	metal ion binding
B	0004322	molecular_function	ferroxidase activity
B	0005506	molecular_function	iron ion binding
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006826	biological_process	iron ion transport
B	0006879	biological_process	intracellular iron ion homeostasis
B	0008199	molecular_function	ferric iron binding
B	0010039	biological_process	response to iron ion
B	0016491	molecular_function	oxidoreductase activity
B	0020037	molecular_function	heme binding
B	0046872	molecular_function	metal ion binding
C	0004322	molecular_function	ferroxidase activity
C	0005506	molecular_function	iron ion binding
C	0005576	cellular_component	extracellular region
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006826	biological_process	iron ion transport
C	0006879	biological_process	intracellular iron ion homeostasis
C	0008199	molecular_function	ferric iron binding
C	0010039	biological_process	response to iron ion
C	0016491	molecular_function	oxidoreductase activity
C	0020037	molecular_function	heme binding
C	0046872	molecular_function	metal ion binding
D	0004322	molecular_function	ferroxidase activity
D	0005506	molecular_function	iron ion binding
D	0005576	cellular_component	extracellular region
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006826	biological_process	iron ion transport
D	0006879	biological_process	intracellular iron ion homeostasis
D	0008199	molecular_function	ferric iron binding
D	0010039	biological_process	response to iron ion
D	0016491	molecular_function	oxidoreductase activity
D	0020037	molecular_function	heme binding
D	0046872	molecular_function	metal ion binding
E	0004322	molecular_function	ferroxidase activity
E	0005506	molecular_function	iron ion binding
E	0005576	cellular_component	extracellular region
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0005886	cellular_component	plasma membrane
E	0006826	biological_process	iron ion transport
E	0006879	biological_process	intracellular iron ion homeostasis
E	0008199	molecular_function	ferric iron binding
E	0010039	biological_process	response to iron ion
E	0016491	molecular_function	oxidoreductase activity
E	0020037	molecular_function	heme binding
E	0046872	molecular_function	metal ion binding
F	0004322	molecular_function	ferroxidase activity
F	0005506	molecular_function	iron ion binding
F	0005576	cellular_component	extracellular region
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0005886	cellular_component	plasma membrane
F	0006826	biological_process	iron ion transport
F	0006879	biological_process	intracellular iron ion homeostasis
F	0008199	molecular_function	ferric iron binding
F	0010039	biological_process	response to iron ion
F	0016491	molecular_function	oxidoreductase activity
F	0020037	molecular_function	heme binding
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 201

Chain	Residue
A	GLU47
A	GLU51
A	GLU94
A	GLU127
A	HIS130

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE A 202

Chain	Residue
A	GLU18
A	GLU51
A	HIS54
A	GLU127

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE TRS A 203

Chain	Residue
A	LYS122
B	LYS122
B	TRS304
B	HOH421
D	LYS122

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM B 301

Chain	Residue
A	PHE26
A	ARG45
A	PHE49
A	MET52
A	GLU56
B	ASN23
B	PHE26
B	PHE49
B	MET52
B	ARG53
B	GLU56
B	TYR71

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE B 302

Chain	Residue
B	GLU18
B	GLU51
B	HIS54
B	GLU127

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE B 303

Chain	Residue
B	GLU47
B	GLU51
B	GLU94
B	GLU127
B	HIS130

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE TRS B 304

Chain	Residue
A	VAL118
A	GLU121
A	TRS203
B	VAL118
B	HOH421
D	VAL118

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE C 201

Chain	Residue
C	GLU18
C	GLU51
C	HIS54
C	GLU127

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE C 202

Chain	Residue
C	GLU47
C	GLU51
C	GLU94
C	GLU127
C	HIS130

site_id	BC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM D 201

Chain	Residue
C	LEU19
C	ILE22
C	PHE26
C	PHE49
C	MET52
C	ARG53
C	GLU56
D	ILE22
D	ASN23
D	PHE26
D	PHE49
D	MET52
D	ARG53

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE D 202

Chain	Residue
D	GLU18
D	GLU51
D	HIS54
D	GLU127
D	FE203

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE D 203

Chain	Residue
D	GLU51
D	GLU94
D	GLU127
D	FE202

site_id	BC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM E 301

Chain	Residue
E	ILE22
E	ASN23
E	PHE26
E	ARG45
E	PHE49
E	MET52
E	ARG53
F	LEU19
F	ILE22
F	PHE26
F	PHE49
F	MET52
F	ARG53
F	ALA55
F	GLU56

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FE E 302

Chain	Residue
E	GLU51
E	GLU94
E	GLU127

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE E 303

Chain	Residue
E	GLU18
E	HIS54
E	ILE123
E	GLU127

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE F 201

Chain	Residue
F	TYR25
F	GLU51
F	GLU94
F	GLU127
F	HIS130

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE F 202

Chain	Residue
F	GLU18
F	GLU51
F	HIS54
F	GLU127

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE TRS F 203

Chain	Residue
C	LYS122
E	VAL118
F	VAL118
F	LYS122
F	HOH309
F	HOH310

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	864
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	36
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
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)