Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4E6K

2.0 A resolution structure of Pseudomonas aeruginosa bacterioferritin (BfrB) in complex with bacterioferritin associated ferredoxin (Bfd)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004322	molecular_function	ferroxidase activity
A	0005506	molecular_function	iron ion binding
A	0005737	cellular_component	cytoplasm
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	0070288	cellular_component	ferritin complex
A	0140315	molecular_function	iron ion sequestering activity
B	0004322	molecular_function	ferroxidase activity
B	0005506	molecular_function	iron ion binding
B	0005737	cellular_component	cytoplasm
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	0070288	cellular_component	ferritin complex
B	0140315	molecular_function	iron ion sequestering activity
C	0004322	molecular_function	ferroxidase activity
C	0005506	molecular_function	iron ion binding
C	0005737	cellular_component	cytoplasm
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	0070288	cellular_component	ferritin complex
C	0140315	molecular_function	iron ion sequestering activity
D	0004322	molecular_function	ferroxidase activity
D	0005506	molecular_function	iron ion binding
D	0005737	cellular_component	cytoplasm
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	0070288	cellular_component	ferritin complex
D	0140315	molecular_function	iron ion sequestering activity
E	0004322	molecular_function	ferroxidase activity
E	0005506	molecular_function	iron ion binding
E	0005737	cellular_component	cytoplasm
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	0070288	cellular_component	ferritin complex
E	0140315	molecular_function	iron ion sequestering activity
F	0004322	molecular_function	ferroxidase activity
F	0005506	molecular_function	iron ion binding
F	0005737	cellular_component	cytoplasm
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	0070288	cellular_component	ferritin complex
F	0140315	molecular_function	iron ion sequestering activity
G	0046872	molecular_function	metal ion binding
G	0051536	molecular_function	iron-sulfur cluster binding
G	0051537	molecular_function	2 iron, 2 sulfur cluster binding
H	0046872	molecular_function	metal ion binding
H	0051536	molecular_function	iron-sulfur cluster binding
H	0051537	molecular_function	2 iron, 2 sulfur cluster binding
I	0046872	molecular_function	metal ion binding
I	0051536	molecular_function	iron-sulfur cluster binding
I	0051537	molecular_function	2 iron, 2 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE K A 201

Chain	Residue
A	ASN148
A	ASN148
A	ASN148
A	ASN148
A	GLN151
A	GLN151
A	GLN151
A	GLN151

site_id	AC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEM A 202

Chain	Residue
A	ILE22
A	ASN23
A	PHE26
A	TYR45
A	ILE49
A	MET52
A	LYS53
A	ILE59
A	LEU71
A	HOH308
A	HOH363
A	HOH387
A	HOH471
A	HOH472
B	LEU19
B	ILE22
B	ASN23
B	PHE26
B	TYR45
B	ILE49
B	MET52
B	LYS53
B	ILE59
A	LEU19

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

Chain	Residue
A	ASP34
A	ASP132
A	THR136
A	HOH464
A	HOH465

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE K B 201

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

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA B 202

Chain	Residue
B	ASP132
B	THR136
B	HOH307
C	ASP34
C	HOH441

site_id	AC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM C 201

Chain	Residue
C	LEU19
C	ILE22
C	ASN23
C	PHE26
C	TYR45
C	ILE49
C	MET52
C	LYS53
C	ALA55
C	ILE59
C	HOH318
C	HOH352
C	HOH359
C	HOH368
D	LEU19
D	ILE22
D	ASN23
D	PHE26
D	TYR45
D	ILE49
D	MET52
D	LYS53
D	ALA55

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA C 202

Chain	Residue
C	ASP132
C	THR136
C	HOH304
E	ASP34
E	HOH446

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA D 201

Chain	Residue
B	ASP34
D	ASP132
D	THR136
D	HOH427
D	HOH428

site_id	AC9
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM E 201

Chain	Residue
F	PHE26
F	TYR45
F	ILE49
F	MET52
F	LYS53
F	LEU71
E	LEU19
E	ASN23
E	PHE26
E	TYR45
E	ILE49
E	MET52
E	LYS53
E	LEU71
E	HOH342
E	HOH366
E	HOH368
E	HOH389
E	HOH395
F	LEU19
F	ILE22
F	ASN23

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA E 202

Chain	Residue
D	ASP34
E	ASP132
E	THR136
E	HOH302
E	HOH447

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE K F 201

Chain	Residue
F	ASN148
F	ASN148
F	ASN148
F	ASN148
F	GLN151
F	GLN151
F	GLN151
F	GLN151

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA F 202

Chain	Residue
F	ASP34
F	ASP132
F	THR136
F	HOH465
F	HOH467

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES G 101

Chain	Residue
G	CYS4
G	LEU5
G	CYS6
G	GLY35
G	GLN37
G	CYS38
G	GLY39
G	CYS41

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 G 102

Chain	Residue
B	LYS76
B	HOH321
G	ARG26
G	ARG29
G	LYS46
G	HOH217
G	HOH226

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES H 101

Chain	Residue
H	CYS4
H	LEU5
H	CYS6
H	GLY35
H	GLN37
H	CYS38
H	GLY39
H	CYS41

site_id	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES I 101

Chain	Residue
I	CYS4
I	LEU5
I	CYS6
I	GLY35
I	GLN37
I	CYS38
I	GLY39
I	CYS41

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	MET1-LEU19

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: {"evidences":[{"source":"PubMed","id":"20067302","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25640193","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3IS8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TOH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D8P","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20067302","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22812654","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25640193","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3IS8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4E6K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TOH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D8P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7K5E","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20067302","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22812654","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25640193","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3IS7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4E6K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TOH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D8P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7K5E","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22812654","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30183257","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4E6K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6E6Q","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22812654","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4E6K","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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