Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004322 | molecular_function | ferroxidase activity |
A | 0005506 | molecular_function | iron ion 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 | 0020037 | molecular_function | heme binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0004322 | molecular_function | ferroxidase activity |
B | 0005506 | molecular_function | iron ion 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 | 0020037 | molecular_function | heme binding |
B | 0046872 | molecular_function | metal ion binding |
C | 0004322 | molecular_function | ferroxidase activity |
C | 0005506 | molecular_function | iron ion binding |
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 | 0020037 | molecular_function | heme binding |
C | 0046872 | molecular_function | metal ion binding |
D | 0004322 | molecular_function | ferroxidase activity |
D | 0005506 | molecular_function | iron ion binding |
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 | 0020037 | molecular_function | heme binding |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | binding site for residue HEM A 201 |
Chain | Residue |
A | LEU19 |
A | HOH375 |
A | HOH412 |
A | HOH413 |
A | HOH422 |
A | HOH457 |
A | HOH461 |
B | LEU19 |
B | ILE22 |
B | ASN23 |
B | PHE26 |
A | ILE22 |
B | TYR45 |
B | ILE49 |
B | MET52 |
B | LYS53 |
B | LEU71 |
A | ASN23 |
A | PHE26 |
A | TYR45 |
A | ILE49 |
A | MET52 |
A | LYS53 |
A | HOH364 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MPD A 202 |
Chain | Residue |
A | LYS2 |
A | GLY3 |
A | VAL111 |
A | ASP113 |
A | HOH377 |
D | ARG102 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue MPD A 203 |
Chain | Residue |
A | ARG61 |
A | HOH383 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue NA A 204 |
Chain | Residue |
A | THR136 |
A | HOH335 |
A | HOH343 |
C | ASP34 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue K B 201 |
Chain | Residue |
A | ASN148 |
A | GLN151 |
B | ASN148 |
B | GLN151 |
C | ASN148 |
C | GLN151 |
D | ASN148 |
D | GLN151 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue MPD B 202 |
Chain | Residue |
B | LYS2 |
B | GLY3 |
B | ARG102 |
B | VAL111 |
B | ASP113 |
B | HOH366 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue MPD B 203 |
Chain | Residue |
B | GLU60 |
B | ARG61 |
B | HOH306 |
B | HOH354 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue NA B 204 |
Chain | Residue |
A | ASP34 |
A | HOH333 |
B | ASP132 |
B | THR136 |
B | HOH311 |
site_id | AC9 |
Number of Residues | 9 |
Details | binding site for residue SO4 B 205 |
Chain | Residue |
B | ARG117 |
B | ARG117 |
B | ASP118 |
B | ASP118 |
B | ASP118 |
B | LYS121 |
B | LYS121 |
B | LYS121 |
B | HOH314 |
site_id | AD1 |
Number of Residues | 18 |
Details | binding site for residue HEM C 201 |
Chain | Residue |
C | LEU19 |
C | ILE22 |
C | ASN23 |
C | ASN23 |
C | PHE26 |
C | PHE26 |
C | TYR45 |
C | TYR45 |
C | ILE49 |
C | ILE49 |
C | MET52 |
C | MET52 |
C | LYS53 |
C | LYS53 |
C | HOH303 |
C | HOH303 |
C | HOH304 |
C | HOH304 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue MPD C 202 |
Chain | Residue |
C | GLU60 |
C | ARG61 |
C | HOH335 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue NA C 203 |
Chain | Residue |
C | ASP132 |
C | THR136 |
C | HOH317 |
D | ASP34 |
D | HOH457 |
site_id | AD4 |
Number of Residues | 18 |
Details | binding site for residue HEM D 201 |
Chain | Residue |
D | PHE26 |
D | TYR45 |
D | TYR45 |
D | ILE49 |
D | MET52 |
D | MET52 |
D | LYS53 |
D | LYS53 |
D | LEU71 |
D | HOH301 |
D | HOH301 |
D | HOH307 |
D | HOH307 |
D | LEU19 |
D | ILE22 |
D | ASN23 |
D | ASN23 |
D | PHE26 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue MPD D 202 |
Chain | Residue |
D | LYS2 |
D | GLY3 |
D | VAL111 |
D | ASP113 |
D | HOH342 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue MPD D 203 |
Chain | Residue |
D | ARG61 |
D | HOH310 |
D | HOH416 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue NA D 204 |
Chain | Residue |
B | ASP34 |
B | HOH454 |
D | ASP132 |
D | THR136 |
D | HOH455 |
site_id | AD8 |
Number of Residues | 12 |
Details | binding site for residue SO4 D 205 |
Chain | Residue |
A | ARG117 |
A | ASP118 |
A | LYS121 |
C | ARG117 |
C | ASP118 |
C | LYS121 |
D | ARG117 |
D | ASP118 |
D | LYS121 |
D | HOH317 |
D | HOH325 |
D | HOH354 |
Functional Information from PROSITE/UniProt
site_id | PS00549 |
Number of Residues | 19 |
Details | BACTERIOFERRITIN Bacterioferritin signature. MkGdkkVIqhLnkiLgneL |
Chain | Residue | Details |
A | MET1-LEU19 | |