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 | 0006826 | biological_process | iron ion transport |
A | 0006879 | biological_process | intracellular iron ion homeostasis |
A | 0006880 | biological_process | intracellular sequestering of iron ion |
A | 0008199 | molecular_function | ferric iron binding |
A | 0015093 | molecular_function | ferrous iron transmembrane transporter activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0020037 | molecular_function | heme binding |
A | 0034755 | biological_process | iron ion transmembrane transport |
A | 0046872 | molecular_function | metal ion binding |
A | 0070288 | cellular_component | ferritin complex |
B | 0004322 | molecular_function | ferroxidase activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006826 | biological_process | iron ion transport |
B | 0006879 | biological_process | intracellular iron ion homeostasis |
B | 0006880 | biological_process | intracellular sequestering of iron ion |
B | 0008199 | molecular_function | ferric iron binding |
B | 0015093 | molecular_function | ferrous iron transmembrane transporter activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0020037 | molecular_function | heme binding |
B | 0034755 | biological_process | iron ion transmembrane transport |
B | 0046872 | molecular_function | metal ion binding |
B | 0070288 | cellular_component | ferritin complex |
C | 0004322 | molecular_function | ferroxidase activity |
C | 0005506 | molecular_function | iron ion binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006826 | biological_process | iron ion transport |
C | 0006879 | biological_process | intracellular iron ion homeostasis |
C | 0006880 | biological_process | intracellular sequestering of iron ion |
C | 0008199 | molecular_function | ferric iron binding |
C | 0015093 | molecular_function | ferrous iron transmembrane transporter activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0020037 | molecular_function | heme binding |
C | 0034755 | biological_process | iron ion transmembrane transport |
C | 0046872 | molecular_function | metal ion binding |
C | 0070288 | cellular_component | ferritin complex |
D | 0004322 | molecular_function | ferroxidase activity |
D | 0005506 | molecular_function | iron ion binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006826 | biological_process | iron ion transport |
D | 0006879 | biological_process | intracellular iron ion homeostasis |
D | 0006880 | biological_process | intracellular sequestering of iron ion |
D | 0008199 | molecular_function | ferric iron binding |
D | 0015093 | molecular_function | ferrous iron transmembrane transporter activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0020037 | molecular_function | heme binding |
D | 0034755 | biological_process | iron ion transmembrane transport |
D | 0046872 | molecular_function | metal ion binding |
D | 0070288 | cellular_component | ferritin complex |
E | 0004322 | molecular_function | ferroxidase activity |
E | 0005506 | molecular_function | iron ion binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0006826 | biological_process | iron ion transport |
E | 0006879 | biological_process | intracellular iron ion homeostasis |
E | 0006880 | biological_process | intracellular sequestering of iron ion |
E | 0008199 | molecular_function | ferric iron binding |
E | 0015093 | molecular_function | ferrous iron transmembrane transporter activity |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0020037 | molecular_function | heme binding |
E | 0034755 | biological_process | iron ion transmembrane transport |
E | 0046872 | molecular_function | metal ion binding |
E | 0070288 | cellular_component | ferritin complex |
F | 0004322 | molecular_function | ferroxidase activity |
F | 0005506 | molecular_function | iron ion binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0005829 | cellular_component | cytosol |
F | 0006826 | biological_process | iron ion transport |
F | 0006879 | biological_process | intracellular iron ion homeostasis |
F | 0006880 | biological_process | intracellular sequestering of iron ion |
F | 0008199 | molecular_function | ferric iron binding |
F | 0015093 | molecular_function | ferrous iron transmembrane transporter activity |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0020037 | molecular_function | heme binding |
F | 0034755 | biological_process | iron ion transmembrane transport |
F | 0046872 | molecular_function | metal ion binding |
F | 0070288 | cellular_component | ferritin complex |
G | 0046872 | molecular_function | metal ion binding |
G | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
H | 0046872 | molecular_function | metal ion binding |
H | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
I | 0046872 | molecular_function | metal ion 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 | 36 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20067302, ECO:0000269|PubMed:25640193, ECO:0007744|PDB:3IS8, ECO:0007744|PDB:4TOH, ECO:0007744|PDB:5D8P |
Chain | Residue | Details |
A | GLU18 | |
B | GLU94 | |
B | GLU127 | |
B | HIS130 | |
C | GLU18 | |
C | GLU51 | |
C | HIS54 | |
C | GLU94 | |
C | GLU127 | |
C | HIS130 | |
D | GLU18 | |
A | GLU51 | |
D | GLU51 | |
D | HIS54 | |
D | GLU94 | |
D | GLU127 | |
D | HIS130 | |
E | GLU18 | |
E | GLU51 | |
E | HIS54 | |
E | GLU94 | |
E | GLU127 | |
A | HIS54 | |
E | HIS130 | |
F | GLU18 | |
F | GLU51 | |
F | HIS54 | |
F | GLU94 | |
F | GLU127 | |
F | HIS130 | |
A | GLU94 | |
A | GLU127 | |
A | HIS130 | |
B | GLU18 | |
B | GLU51 | |
B | HIS54 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:20067302, ECO:0000269|PubMed:22812654, ECO:0000269|PubMed:25640193, ECO:0007744|PDB:3IS8, ECO:0007744|PDB:4E6K, ECO:0007744|PDB:4TOH, ECO:0007744|PDB:5D8P, ECO:0007744|PDB:7K5E |
Chain | Residue | Details |
A | MET52 | |
B | MET52 | |
C | MET52 | |
D | MET52 | |
E | MET52 | |
F | MET52 | |
I | ARG26 | |
I | ARG29 | |
I | LYS46 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20067302, ECO:0000269|PubMed:22812654, ECO:0000269|PubMed:25640193, ECO:0007744|PDB:3IS7, ECO:0007744|PDB:4E6K, ECO:0007744|PDB:4TOH, ECO:0007744|PDB:5D8P, ECO:0007744|PDB:7K5E |
Chain | Residue | Details |
A | ASN148 | |
E | GLN151 | |
F | ASN148 | |
F | GLN151 | |
A | GLN151 | |
B | ASN148 | |
B | GLN151 | |
C | ASN148 | |
C | GLN151 | |
D | ASN148 | |
D | GLN151 | |
E | ASN148 |