Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4TOG

1.80A resolution structure of BfrB (C89S, K96C) crystal form 2 from Pseudomonas aeruginosa

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	binding site for residue HEM A 201

Chain	Residue
A	LEU19
A	HOH375
A	HOH412
A	HOH413
A	HOH422
A	HOH457
A	HOH461
B	LEU19
B	ILE22
B	ASN23
B	PHE26
A	ILE22
B	TYR45
B	ILE49
B	MET52
B	LYS53
B	LEU71
A	ASN23
A	PHE26
A	TYR45
A	ILE49
A	MET52
A	LYS53
A	HOH364

site_id	AC2
Number of Residues	6
Details	binding site for residue MPD A 202

Chain	Residue
A	LYS2
A	GLY3
A	VAL111
A	ASP113
A	HOH377
D	ARG102

site_id	AC3
Number of Residues	2
Details	binding site for residue MPD A 203

Chain	Residue
A	ARG61
A	HOH383

site_id	AC4
Number of Residues	4
Details	binding site for residue NA A 204

Chain	Residue
A	THR136
A	HOH335
A	HOH343
C	ASP34

site_id	AC5
Number of Residues	8
Details	binding site for residue K B 201

Chain	Residue
A	ASN148
A	GLN151
B	ASN148
B	GLN151
C	ASN148
C	GLN151
D	ASN148
D	GLN151

site_id	AC6
Number of Residues	6
Details	binding site for residue MPD B 202

Chain	Residue
B	LYS2
B	GLY3
B	ARG102
B	VAL111
B	ASP113
B	HOH366

site_id	AC7
Number of Residues	4
Details	binding site for residue MPD B 203

Chain	Residue
B	GLU60
B	ARG61
B	HOH306
B	HOH354

site_id	AC8
Number of Residues	5
Details	binding site for residue NA B 204

Chain	Residue
A	ASP34
A	HOH333
B	ASP132
B	THR136
B	HOH311

site_id	AC9
Number of Residues	9
Details	binding site for residue SO4 B 205

Chain	Residue
B	ARG117
B	ARG117
B	ASP118
B	ASP118
B	ASP118
B	LYS121
B	LYS121
B	LYS121
B	HOH314

site_id	AD1
Number of Residues	18
Details	binding site for residue HEM C 201

Chain	Residue
C	LEU19
C	ILE22
C	ASN23
C	ASN23
C	PHE26
C	PHE26
C	TYR45
C	TYR45
C	ILE49
C	ILE49
C	MET52
C	MET52
C	LYS53
C	LYS53
C	HOH303
C	HOH303
C	HOH304
C	HOH304

site_id	AD2
Number of Residues	3
Details	binding site for residue MPD C 202

Chain	Residue
C	GLU60
C	ARG61
C	HOH335

site_id	AD3
Number of Residues	5
Details	binding site for residue NA C 203

Chain	Residue
C	ASP132
C	THR136
C	HOH317
D	ASP34
D	HOH457

site_id	AD4
Number of Residues	18
Details	binding site for residue HEM D 201

Chain	Residue
D	PHE26
D	TYR45
D	TYR45
D	ILE49
D	MET52
D	MET52
D	LYS53
D	LYS53
D	LEU71
D	HOH301
D	HOH301
D	HOH307
D	HOH307
D	LEU19
D	ILE22
D	ASN23
D	ASN23
D	PHE26

site_id	AD5
Number of Residues	5
Details	binding site for residue MPD D 202

Chain	Residue
D	LYS2
D	GLY3
D	VAL111
D	ASP113
D	HOH342

site_id	AD6
Number of Residues	3
Details	binding site for residue MPD D 203

Chain	Residue
D	ARG61
D	HOH310
D	HOH416

site_id	AD7
Number of Residues	5
Details	binding site for residue NA D 204

Chain	Residue
B	ASP34
B	HOH454
D	ASP132
D	THR136
D	HOH455

site_id	AD8
Number of Residues	12
Details	binding site for residue SO4 D 205

Chain	Residue
A	ARG117
A	ASP118
A	LYS121
C	ARG117
C	ASP118
C	LYS121
D	ARG117
D	ASP118
D	LYS121
D	HOH317
D	HOH325
D	HOH354

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	576
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	24
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	4
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	8
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

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