Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5D8O

1.90A resolution structure of BfrB (wild-type, C2221 form) 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
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	0004322	molecular_function	ferroxidase activity
G	0005506	molecular_function	iron ion binding
G	0005737	cellular_component	cytoplasm
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	0070288	cellular_component	ferritin complex
G	0140315	molecular_function	iron ion sequestering activity
H	0004322	molecular_function	ferroxidase activity
H	0005506	molecular_function	iron ion binding
H	0005737	cellular_component	cytoplasm
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	0070288	cellular_component	ferritin complex
H	0140315	molecular_function	iron ion sequestering activity
I	0004322	molecular_function	ferroxidase activity
I	0005506	molecular_function	iron ion binding
I	0005737	cellular_component	cytoplasm
I	0005829	cellular_component	cytosol
I	0006811	biological_process	monoatomic ion transport
I	0006826	biological_process	iron ion transport
I	0006879	biological_process	intracellular iron ion homeostasis
I	0008199	molecular_function	ferric iron binding
I	0016491	molecular_function	oxidoreductase activity
I	0020037	molecular_function	heme binding
I	0046872	molecular_function	metal ion binding
I	0070288	cellular_component	ferritin complex
I	0140315	molecular_function	iron ion sequestering activity
J	0004322	molecular_function	ferroxidase activity
J	0005506	molecular_function	iron ion binding
J	0005737	cellular_component	cytoplasm
J	0005829	cellular_component	cytosol
J	0006811	biological_process	monoatomic ion transport
J	0006826	biological_process	iron ion transport
J	0006879	biological_process	intracellular iron ion homeostasis
J	0008199	molecular_function	ferric iron binding
J	0016491	molecular_function	oxidoreductase activity
J	0020037	molecular_function	heme binding
J	0046872	molecular_function	metal ion binding
J	0070288	cellular_component	ferritin complex
J	0140315	molecular_function	iron ion sequestering activity
K	0004322	molecular_function	ferroxidase activity
K	0005506	molecular_function	iron ion binding
K	0005737	cellular_component	cytoplasm
K	0005829	cellular_component	cytosol
K	0006811	biological_process	monoatomic ion transport
K	0006826	biological_process	iron ion transport
K	0006879	biological_process	intracellular iron ion homeostasis
K	0008199	molecular_function	ferric iron binding
K	0016491	molecular_function	oxidoreductase activity
K	0020037	molecular_function	heme binding
K	0046872	molecular_function	metal ion binding
K	0070288	cellular_component	ferritin complex
K	0140315	molecular_function	iron ion sequestering activity
L	0004322	molecular_function	ferroxidase activity
L	0005506	molecular_function	iron ion binding
L	0005737	cellular_component	cytoplasm
L	0005829	cellular_component	cytosol
L	0006811	biological_process	monoatomic ion transport
L	0006826	biological_process	iron ion transport
L	0006879	biological_process	intracellular iron ion homeostasis
L	0008199	molecular_function	ferric iron binding
L	0016491	molecular_function	oxidoreductase activity
L	0020037	molecular_function	heme binding
L	0046872	molecular_function	metal ion binding
L	0070288	cellular_component	ferritin complex
L	0140315	molecular_function	iron ion sequestering activity

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	GLN151
E	ASN148
E	GLN151
J	ASN148
J	GLN151
K	ASN148
K	GLN151

site_id	AC2
Number of Residues	7
Details	binding site for residue PG4 A 202

Chain	Residue
A	GLU60
A	ARG61
A	PHE64
A	VAL115
A	HOH301
L	GLU125
A	LYS57

site_id	AC3
Number of Residues	10
Details	binding site for residue PG4 A 203

Chain	Residue
A	GLU125
A	GLU129
A	ASP132
A	HOH309
A	HOH389
B	ARG61
B	PHE64
B	VAL115
B	HOH360
B	HOH374

site_id	AC4
Number of Residues	5
Details	binding site for residue PG4 A 204

Chain	Residue
A	ASN33
A	LYS38
A	HOH305
J	ASP132
J	THR136

site_id	AC5
Number of Residues	18
Details	binding site for residue HEM A 205

Chain	Residue
A	ASN23
A	PHE26
A	TYR45
A	ILE49
A	MET52
A	LYS53
A	ILE59
A	HOH311
A	HOH312
A	HOH347
G	LEU19
G	ASN23
G	PHE26
G	TYR45
G	ILE49
G	MET52
G	LYS53
G	HOH379

site_id	AC6
Number of Residues	8
Details	binding site for residue K B 201

Chain	Residue
B	ASN148
B	GLN151
C	ASN148
C	GLN151
G	ASN148
G	GLN151
L	ASN148
L	GLN151

site_id	AC7
Number of Residues	4
Details	binding site for residue PG4 B 202

Chain	Residue
B	ASN33
B	LYS38
C	ASP132
C	THR136

site_id	AC8
Number of Residues	23
Details	binding site for residue HEM B 203

Chain	Residue
B	ASN23
B	PHE26
B	TYR45
B	ILE49
B	MET52
B	LYS53
B	ALA55
B	ILE59
B	HOH310
B	HOH323
B	HOH324
B	HOH326
B	HOH327
B	HOH348
B	HOH388
E	LEU19
E	ILE22
E	ASN23
E	PHE26
E	TYR45
E	ILE49
E	MET52
E	LYS53

site_id	AC9
Number of Residues	10
Details	binding site for residue PG4 C 201

Chain	Residue
C	GLU125
C	GLU129
C	ASP132
C	HOH305
C	HOH320
C	HOH331
C	HOH350
E	GLU60
E	ARG61
E	VAL115

site_id	AD1
Number of Residues	4
Details	binding site for residue PG4 C 202

Chain	Residue
C	ASN33
C	LYS38
G	ASP132
G	THR136

site_id	AD2
Number of Residues	8
Details	binding site for residue K D 201

Chain	Residue
F	ASN148
F	GLN151
H	ASN148
H	GLN151
I	ASN148
I	GLN151
D	ASN148
D	GLN151

site_id	AD3
Number of Residues	4
Details	binding site for residue PG4 D 202

Chain	Residue
D	ASN33
D	LYS38
H	ASP132
H	THR136

site_id	AD4
Number of Residues	20
Details	binding site for residue HEM D 203

Chain	Residue
D	LEU19
D	ILE22
D	ASN23
D	ASN23
D	PHE26
D	PHE26
D	TYR45
D	TYR45
D	ILE49
D	ILE49
D	MET52
D	MET52
D	LYS53
D	LYS53
D	LEU71
D	HOH301
D	HOH303
D	HOH303
D	HOH397
D	HOH397

site_id	AD5
Number of Residues	10
Details	binding site for residue PG4 E 201

Chain	Residue
E	GLU125
E	GLU128
E	GLU129
E	ASP132
E	HOH315
E	HOH321
E	HOH376
E	HOH401
F	ARG61
F	VAL115

site_id	AD6
Number of Residues	4
Details	binding site for residue PG4 E 202

Chain	Residue
A	ASP132
A	THR136
E	ASN33
E	LYS38

site_id	AD7
Number of Residues	9
Details	binding site for residue PG4 F 201

Chain	Residue
C	PHE64
C	VAL115
F	GLU125
F	GLU129
F	ASP132
F	HOH303
F	HOH322
F	HOH333
F	HOH341

site_id	AD8
Number of Residues	5
Details	binding site for residue PG4 F 202

Chain	Residue
D	ASP132
D	THR136
F	ASN33
F	LYS38
F	GLU156

site_id	AD9
Number of Residues	19
Details	binding site for residue HEM F 203

Chain	Residue
F	ASN23
F	PHE26
F	TYR45
F	ILE49
F	MET52
F	LYS53
F	ILE59
F	HOH309
F	HOH310
F	HOH317
F	HOH376
F	HOH383
K	LEU19
K	ASN23
K	PHE26
K	TYR45
K	ILE49
K	MET52
K	LYS53

site_id	AE1
Number of Residues	10
Details	binding site for residue PG4 G 201

Chain	Residue
G	ARG61
G	VAL115
G	LEU119
G	HOH303
G	HOH309
G	HOH338
J	GLU125
J	GLU128
J	GLU129
J	ASP132

site_id	AE2
Number of Residues	10
Details	binding site for residue PG4 G 202

Chain	Residue
G	GLU125
G	GLU129
G	ASP132
G	HOH307
G	HOH311
G	HOH315
I	GLU60
I	ARG61
I	VAL115
I	LEU119

site_id	AE3
Number of Residues	5
Details	binding site for residue PG4 G 203

Chain	Residue
G	ASN33
G	LYS38
G	HOH344
L	ASP132
L	THR136

site_id	AE4
Number of Residues	10
Details	binding site for residue PG4 H 201

Chain	Residue
D	GLU60
D	ARG61
D	PHE64
H	GLU125
H	GLU129
H	ASP132
H	HOH306
H	HOH307
H	HOH326
H	HOH381

site_id	AE5
Number of Residues	8
Details	binding site for residue PG4 H 202

Chain	Residue
H	GLU60
H	ARG61
H	VAL115
H	HOH308
H	HOH328
K	GLU125
K	GLU129
K	ASP132

site_id	AE6
Number of Residues	5
Details	binding site for residue PG4 H 203

Chain	Residue
H	ASN33
H	LYS38
H	HOH352
I	ASP132
I	THR136

site_id	AE7
Number of Residues	4
Details	binding site for residue PG4 I 201

Chain	Residue
F	ASP132
F	THR136
I	ASN33
I	LYS38

site_id	AE8
Number of Residues	22
Details	binding site for residue HEM I 202

Chain	Residue
C	ASN23
C	PHE26
C	TYR45
C	ILE49
C	MET52
C	LYS53
C	ALA55
C	ILE59
I	LEU19
I	ILE22
I	ASN23
I	PHE26
I	TYR45
I	ILE49
I	MET52
I	LYS53
I	HOH313
I	HOH315
I	HOH316
I	HOH326
I	HOH333
I	HOH396

site_id	AE9
Number of Residues	11
Details	binding site for residue PG4 J 201

Chain	Residue
I	GLU125
I	GLU129
I	ASP132
J	ARG61
J	PHE64
J	VAL115
J	LEU119
J	HOH310
J	HOH340
J	HOH357
J	HOH391

site_id	AF1
Number of Residues	5
Details	binding site for residue PG4 J 202

Chain	Residue
J	ASN33
J	LYS38
J	HOH328
K	ASP132
K	THR136

site_id	AF2
Number of Residues	9
Details	binding site for residue PG4 J 203

Chain	Residue
A	TRP35
A	GLU81
F	GLN110
F	HOH364
J	GLN142
J	LYS143
J	HOH364
J	HOH380
J	HOH405

site_id	AF3
Number of Residues	21
Details	binding site for residue HEM J 204

Chain	Residue
H	ASN23
H	PHE26
H	TYR45
H	ILE49
H	MET52
H	LYS53
H	ILE59
J	LEU19
J	ILE22
J	ASN23
J	PHE26
J	TYR45
J	ILE49
J	MET52
J	LYS53
J	HOH302
J	HOH314
J	HOH318
J	HOH321
J	HOH329
J	HOH359

site_id	AF4
Number of Residues	8
Details	binding site for residue PG4 K 201

Chain	Residue
D	GLU125
D	ASP132
K	GLU60
K	ARG61
K	PHE64
K	VAL115
K	HOH337
K	HOH339

site_id	AF5
Number of Residues	4
Details	binding site for residue PG4 K 202

Chain	Residue
E	ASP132
E	THR136
K	ASN33
K	LYS38

site_id	AF6
Number of Residues	11
Details	binding site for residue PG4 L 201

Chain	Residue
B	GLU125
B	GLU129
B	ASP132
L	GLU60
L	PHE64
L	VAL115
L	LEU119
L	HOH305
L	HOH334
L	HOH340
L	HOH357

site_id	AF7
Number of Residues	5
Details	binding site for residue PG4 L 202

Chain	Residue
B	ASP132
B	THR136
L	ASN33
L	LYS38
L	HOH304

site_id	AF8
Number of Residues	20
Details	binding site for residue HEM L 203

Chain	Residue
L	LEU19
L	ILE22
L	ASN23
L	ASN23
L	PHE26
L	PHE26
L	TYR45
L	TYR45
L	ILE49
L	ILE49
L	MET52
L	MET52
L	LYS53
L	LYS53
L	ILE59
L	LEU71
L	HOH303
L	HOH303
L	HOH306
L	HOH306

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	1728
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	72
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	12
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	24
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)