Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004322 | molecular_function | ferroxidase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006826 | biological_process | iron ion transport |
A | 0006879 | biological_process | intracellular iron ion homeostasis |
A | 0008198 | molecular_function | ferrous iron binding |
A | 0008199 | molecular_function | ferric iron binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue MG A 201 |
Chain | Residue |
A | GLU23 |
A | GLU58 |
A | HIS61 |
A | HOH340 |
A | HOH342 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue MG A 202 |
Chain | Residue |
A | HOH558 |
A | HOH558 |
A | HOH612 |
A | HOH612 |
A | HOH313 |
A | HOH313 |
A | HOH319 |
A | HOH319 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MG A 203 |
Chain | Residue |
A | HOH434 |
A | HOH553 |
A | HOH562 |
A | HOH583 |
A | HOH634 |
A | HOH643 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MG A 204 |
Chain | Residue |
A | HOH309 |
A | HOH375 |
A | HOH514 |
A | HOH538 |
A | HOH610 |
A | HOH626 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MG A 205 |
Chain | Residue |
A | HOH388 |
A | HOH427 |
A | HOH430 |
A | HOH483 |
A | HOH599 |
A | HOH636 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue MG A 206 |
Chain | Residue |
A | SER10 |
A | HOH345 |
A | HOH421 |
A | HOH469 |
A | HOH481 |
A | HOH604 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue MG A 207 |
Chain | Residue |
A | HOH335 |
A | HOH335 |
A | HOH335 |
A | HOH522 |
A | HOH522 |
A | HOH522 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue MG A 208 |
Chain | Residue |
A | ASP127 |
A | ASP127 |
A | ASP127 |
A | HOH304 |
A | HOH304 |
A | HOH304 |
A | HOH305 |
A | HOH305 |
A | HOH305 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue CL A 209 |
Chain | Residue |
A | HIS169 |
A | HIS169 |
A | HIS169 |
A | HIS169 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue CL A 210 |
Chain | Residue |
A | ASP87 |
A | HOH315 |
A | HOH640 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue CL A 211 |
Chain | Residue |
A | GLN101 |
A | LEU102 |
A | THR105 |
A | HOH598 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue CL A 212 |
Chain | Residue |
A | ASN17 |
A | HOH529 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue CL A 213 |
Chain | Residue |
A | ARG5 |
A | ASN7 |
A | TYR8 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue CL A 214 |
Chain | Residue |
A | HIS169 |
A | HIS169 |
A | HIS169 |
A | HIS169 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue CL A 215 |
Chain | Residue |
A | SER10 |
A | HOH555 |
A | HOH580 |
A | HOH596 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue CL A 216 |
Chain | Residue |
A | ASN7 |
A | GLN108 |
A | LYS115 |
A | HOH320 |
A | HOH453 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue CL A 217 |
Chain | Residue |
A | SER131 |
A | GLU132 |
A | TYR133 |
A | GLU135 |
A | ALA136 |
A | HOH582 |
site_id | AD9 |
Number of Residues | 2 |
Details | binding site for residue CL A 218 |
Chain | Residue |
A | LYS64 |
A | HOH576 |
site_id | AE1 |
Number of Residues | 2 |
Details | binding site for residue CL A 219 |
Chain | Residue |
A | HOH480 |
A | HOH639 |
site_id | AE2 |
Number of Residues | 6 |
Details | binding site for residue CL A 220 |
Chain | Residue |
A | VAL1 |
A | SER2 |
A | ARG5 |
A | GLY73 |
A | HOH355 |
A | HOH581 |
site_id | AE3 |
Number of Residues | 4 |
Details | binding site for residue CL A 221 |
Chain | Residue |
A | HOH371 |
A | HOH463 |
A | LYS82 |
A | LYS82 |
site_id | AE4 |
Number of Residues | 4 |
Details | binding site for residue CL A 222 |
Chain | Residue |
A | ASN150 |
A | LYS168 |
A | SER170 |
A | HOH416 |
Functional Information from PROSITE/UniProt
site_id | PS00204 |
Number of Residues | 21 |
Details | FERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFLEseYLeaqvkaIK |
Chain | Residue | Details |
A | ASP122-LYS142 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 149 |
Details | Domain: {"description":"Ferritin-like diiron","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | Binding site: {} |