3E2C
Escherichia coli Bacterioferritin Mutant E128R/E135R
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004322 | molecular_function | ferroxidase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0005515 | molecular_function | protein binding |
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 | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0020037 | molecular_function | heme binding |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0140315 | molecular_function | iron ion sequestering activity |
B | 0004322 | molecular_function | ferroxidase activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0005515 | molecular_function | protein binding |
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 | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0020037 | molecular_function | heme binding |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0140315 | molecular_function | iron ion sequestering activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 200 |
Chain | Residue |
A | GLU18 |
A | GLU51 |
A | HIS54 |
A | GLU127 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 201 |
Chain | Residue |
A | ARG117 |
A | ARG155 |
A | HOH430 |
B | ARG125 |
B | ARG128 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 202 |
Chain | Residue |
A | ARG39 |
A | TRP133 |
A | ARG135 |
A | HOH362 |
A | HOH427 |
A | HOH428 |
A | HOH441 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 200 |
Chain | Residue |
B | GLU18 |
B | GLU51 |
B | HIS54 |
B | GLU127 |
site_id | AC5 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE HEM A 203 |
Chain | Residue |
A | LEU19 |
A | ASN23 |
A | PHE26 |
A | TYR45 |
A | ILE49 |
A | MET52 |
A | LYS53 |
A | HOH330 |
A | HOH358 |
A | HOH414 |
B | ILE22 |
B | ASN23 |
B | TYR45 |
B | ILE49 |
B | MET52 |
B | ALA55 |
B | ASP56 |
B | ILE59 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM A 204 |
Chain | Residue |
A | LEU19 |
A | ILE22 |
A | ASN23 |
A | TYR45 |
A | ILE49 |
A | MET52 |
A | ALA55 |
A | ASP56 |
A | ILE59 |
A | HOH330 |
A | HOH358 |
A | HOH368 |
A | HOH414 |
B | LEU19 |
B | PHE26 |
B | TYR45 |
B | ILE49 |
B | MET52 |
B | LYS53 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO A 301 |
Chain | Residue |
A | LEU14 |
A | ASN17 |
A | GLU18 |
A | TYR58 |
A | GLY97 |
A | ILE123 |
A | GLU127 |
A | HOH309 |
A | HOH315 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 302 |
Chain | Residue |
A | GLU47 |
A | ASP50 |
A | GLU51 |
A | HIS54 |
A | GLU94 |
A | GLU127 |
A | HIS130 |
A | HOH415 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO B 301 |
Chain | Residue |
B | LEU14 |
B | ASN17 |
B | GLU18 |
B | TYR58 |
B | GLY97 |
B | LEU101 |
B | ILE123 |
B | GLU127 |
B | HOH329 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 302 |
Chain | Residue |
B | GLU47 |
B | ASP50 |
B | GLU51 |
B | GLU94 |
B | GLU127 |
B | HIS130 |
Functional Information from PROSITE/UniProt
site_id | PS00549 |
Number of Residues | 19 |
Details | BACTERIOFERRITIN Bacterioferritin signature. MkGdtkVInyLnklLgneL |
Chain | Residue | Details |
A | MET1-LEU19 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 |
Chain | Residue | Details |
A | GLU18 | |
B | HIS46 | |
B | ASP50 | |
B | GLU51 | |
B | HIS54 | |
B | GLU94 | |
B | GLU127 | |
B | HIS130 | |
A | HIS46 | |
A | ASP50 | |
A | GLU51 | |
A | HIS54 | |
A | GLU94 | |
A | GLU127 | |
A | HIS130 | |
B | GLU18 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 |
Chain | Residue | Details |
A | MET52 | |
B | MET52 |