3ISF

Structure of non-mineralized Bfrb (as-isolated) from Pseudomonas aeruginosa to 2.07A Resolution

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE K A 159

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

---

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM B 159

Chain	Residue
A	PHE26
A	TYR45
A	ILE49
A	MET52
A	LYS53
B	LEU19
B	ILE22
B	ASN23
B	PHE26
B	TYR45
B	ILE49
B	MET52
B	LYS53
B	HOH355
B	HOH360
B	HOH361
A	ASN23

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE K B 160

Chain	Residue
B	ASN148
B	GLN151
C	ASN148
C	GLN151
E	ASN148
E	GLN151
F	ASN148
F	GLN151

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM C 159

Chain	Residue
C	ILE22
C	ASN23
C	PHE26
C	TYR45
C	ILE49
C	MET52
C	LYS53
C	HOH362
C	HOH363
D	ASN23
D	PHE26
D	TYR45
D	ILE49
D	MET52
D	LYS53

---

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM E 159

Chain	Residue
E	LEU19
E	ILE22
E	ASN23
E	ASN23
E	PHE26
E	PHE26
E	TYR45
E	TYR45
E	ILE49
E	ILE49
E	MET52
E	MET52
E	LYS53
E	HOH171
E	HOH171

---

site_id	AC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM F 159

Chain	Residue
F	LEU19
F	ILE22
F	ILE22
F	ASN23
F	ASN23
F	PHE26
F	PHE26
F	TYR45
F	TYR45
F	ILE49
F	ILE49
F	MET52
F	MET52
F	LYS53
F	LYS53
F	ALA55
F	HOH189
F	HOH189
F	HOH359
F	HOH359

---

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	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_FI2
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_FI3
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_FI4
Number of Residues	144
Details	Domain: {"description":"Ferritin-like diiron","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---