Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6NLM

1.90 A resolution structure of WT BfrB from Pseudomonas aeruginosa in complex with a protein-protein interaction inhibitor (analog 15)

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 FE2 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	10
Details	binding site for residue KT1 A 202

Chain	Residue
A	PRO69
A	LEU71
A	GLN72
A	HOH304
D	ASN82
D	GLN84
D	GLU85
G	LEU27
G	ILE79
A	LEU68

site_id	AC3
Number of Residues	16
Details	binding site for residue HEM A 203

Chain	Residue
A	ASN23
A	PHE26
A	TYR45
A	ILE49
A	MET52
A	LYS53
A	ILE59
A	HOH303
A	HOH353
G	LEU19
G	ASN23
G	PHE26
G	TYR45
G	ILE49
G	MET52
G	LYS53

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

Chain	Residue
A	ASN33
A	LYS38
A	HOH354
J	ASP132
J	THR136

site_id	AC5
Number of Residues	8
Details	binding site for residue FE2 B 201

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

site_id	AC6
Number of Residues	9
Details	binding site for residue KT1 B 202

Chain	Residue
B	LEU63
B	LEU68
B	PRO69
B	LEU71
B	GLN72
E	LEU27
E	MET31
E	ILE79
E	GLY80

site_id	AC7
Number of Residues	17
Details	binding site for residue HEM B 203

Chain	Residue
B	ASN23
B	PHE26
B	TYR45
B	ILE49
B	MET52
B	LYS53
B	ILE59
B	HOH303
B	HOH306
B	HOH320
E	LEU19
E	ASN23
E	PHE26
E	TYR45
E	ILE49
E	MET52
E	LYS53

site_id	AC8
Number of Residues	6
Details	binding site for residue PG4 B 204

Chain	Residue
B	ASN33
B	LYS38
B	HOH340
B	HOH387
C	ASP132
C	THR136

site_id	AC9
Number of Residues	3
Details	binding site for residue PG4 B 205

Chain	Residue
B	LYS143
L	TRP35
L	ASN82

site_id	AD1
Number of Residues	3
Details	binding site for residue PG4 B 206

Chain	Residue
B	LYS6
B	HIS10
B	HOH361

site_id	AD2
Number of Residues	10
Details	binding site for residue KT1 C 201

Chain	Residue
C	LEU63
C	LEU68
C	PRO69
C	LEU71
C	GLN72
I	LEU27
I	TRP35
I	ILE79
I	GLY80
I	GLU81

site_id	AD3
Number of Residues	17
Details	binding site for residue HEM C 202

Chain	Residue
C	MET52
C	LYS53
C	ILE59
C	HOH307
C	HOH312
I	LEU19
I	ILE22
I	ASN23
I	PHE26
I	TYR45
I	ILE49
I	MET52
I	LYS53
C	ASN23
C	PHE26
C	TYR45
C	ILE49

site_id	AD4
Number of Residues	5
Details	binding site for residue PG4 C 203

Chain	Residue
C	ASN33
C	LYS38
G	ASP132
G	THR136
G	HOH358

site_id	AD5
Number of Residues	8
Details	binding site for residue FE2 D 201

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

site_id	AD6
Number of Residues	10
Details	binding site for residue KT1 D 202

Chain	Residue
D	LEU27
D	LEU68
D	PRO69
D	LEU71
D	GLN72
D	ILE79
D	HOH307
G	ASN82
G	GLN84
G	GLU85

site_id	AD7
Number of Residues	14
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	HOH305

site_id	AD8
Number of Residues	4
Details	binding site for residue PG4 D 204

Chain	Residue
D	ASN33
D	LYS38
H	ASP132
H	THR136

site_id	AD9
Number of Residues	3
Details	binding site for residue PG4 D 205

Chain	Residue
D	LYS143
F	TRP35
F	GLU81

site_id	AE1
Number of Residues	10
Details	binding site for residue KT1 E 201

Chain	Residue
B	LEU27
B	MET31
B	TRP35
B	ILE79
B	GLY80
B	GLU81
E	LEU68
E	PRO69
E	LEU71
E	GLN72

site_id	AE2
Number of Residues	5
Details	binding site for residue PG4 E 202

Chain	Residue
A	ASP132
A	THR136
E	ASN33
E	LYS38
E	HOH374

site_id	AE3
Number of Residues	4
Details	binding site for residue PG4 E 203

Chain	Residue
E	LYS143
E	HOH307
K	TRP35
K	GLU81

site_id	AE4
Number of Residues	7
Details	binding site for residue KT1 F 201

Chain	Residue
F	LEU68
F	PRO69
F	LEU71
F	GLN72
K	LEU27
K	MET31
K	TRP35

site_id	AE5
Number of Residues	17
Details	binding site for residue HEM F 202

Chain	Residue
F	LEU19
F	ASN23
F	TYR45
F	ILE49
F	MET52
F	LYS53
F	ILE59
F	HOH301
F	HOH321
F	HOH333
K	LEU19
K	ASN23
K	PHE26
K	TYR45
K	ILE49
K	MET52
K	LYS53

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

Chain	Residue
D	ASP132
D	THR136
F	ASN33
F	LYS38
F	HOH347

site_id	AE7
Number of Residues	11
Details	binding site for residue KT1 G 201

Chain	Residue
A	LEU27
A	MET31
A	TRP35
A	ILE79
A	GLU81
G	LEU63
G	LEU68
G	PRO69
G	LEU71
G	GLN72
G	HOH305

site_id	AE8
Number of Residues	4
Details	binding site for residue PG4 G 202

Chain	Residue
G	ASN33
G	LYS38
L	ASP132
L	THR136

site_id	AE9
Number of Residues	9
Details	binding site for residue KT1 H 201

Chain	Residue
H	LEU68
H	PRO69
H	LEU71
H	GLN72
H	HOH321
J	LEU27
J	TRP35
J	ILE79
J	GLY80

site_id	AF1
Number of Residues	17
Details	binding site for residue HEM H 202

Chain	Residue
H	ASN23
H	PHE26
H	TYR45
H	ILE49
H	MET52
H	LYS53
H	ILE59
H	HOH311
H	HOH317
J	LEU19
J	ILE22
J	ASN23
J	PHE26
J	TYR45
J	ILE49
J	MET52
J	LYS53

site_id	AF2
Number of Residues	6
Details	binding site for residue PG4 H 203

Chain	Residue
H	ASN33
H	LYS38
H	HOH361
H	HOH380
I	ASP132
I	THR136

site_id	AF3
Number of Residues	3
Details	binding site for residue PG4 H 204

Chain	Residue
H	LYS6
H	GLN9
H	HIS10

site_id	AF4
Number of Residues	9
Details	binding site for residue KT1 I 201

Chain	Residue
C	LEU27
C	MET31
C	TRP35
C	ILE79
C	GLY80
I	LEU68
I	PRO69
I	LEU71
I	GLN72

site_id	AF5
Number of Residues	5
Details	binding site for residue PG4 I 202

Chain	Residue
F	ASP132
F	THR136
F	HOH360
I	ASN33
I	LYS38

site_id	AF6
Number of Residues	9
Details	binding site for residue KT1 J 201

Chain	Residue
H	LEU27
H	MET31
H	TRP35
H	ILE79
H	GLY80
J	LEU68
J	PRO69
J	LEU71
J	GLN72

site_id	AF7
Number of Residues	9
Details	binding site for residue PG4 J 202

Chain	Residue
A	TRP35
A	GLU81
F	GLN110
J	GLN142
J	LYS143
J	HOH339
J	HOH350
J	HOH372
J	HOH392

site_id	AF8
Number of Residues	7
Details	binding site for residue PG4 J 203

Chain	Residue
J	ASN33
J	LYS38
J	HOH327
K	ASP132
K	THR136
K	GLN137
K	HOH384

site_id	AF9
Number of Residues	8
Details	binding site for residue KT1 K 201

Chain	Residue
F	LEU27
F	MET31
F	ILE79
F	GLY80
K	LEU68
K	PRO69
K	LEU71
K	GLN72

site_id	AG1
Number of Residues	4
Details	binding site for residue PG4 K 202

Chain	Residue
E	ASP132
E	THR136
K	ASN33
K	LYS38

site_id	AG2
Number of Residues	9
Details	binding site for residue KT1 L 201

Chain	Residue
L	LEU27
L	MET31
L	TRP35
L	LEU63
L	LEU68
L	PRO69
L	LEU71
L	GLN72
L	ILE79

site_id	AG3
Number of Residues	19
Details	binding site for residue HEM L 202

Chain	Residue
L	LEU19
L	ILE22
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	ILE59
L	LEU71
L	HOH301
L	HOH301
L	HOH302

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)