Equus caballus
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | Protein 24 | CADMIUM ION × 144 water × 24 | Consistent with protein count |
| UniProt name | FRIL_HORSE |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–174； UniProt 1–174 |
The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.
| Entry ID entry_id | 1aew |
| Deposition date deposition_date | 1997-02-26 |
| Structure title title | L-CHAIN HORSE APOFERRITIN |
| Keywords keywords | IRON STORAGE, MULTIGENE FAMILY; IRON STORAGE |
| Experimental Method method | X-RAY DIFFRACTION |
This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.
Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)
| Rg（Guinier） | 54.27 Å |
| Rg (electron density) | 53.42 Å |
| Total Rg | 53.66 Å |
| Atom count | 32856 |
| Residues | 4080 |
| Excluded volume | 585280 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1aewa_ |
| Class class | a — All alpha proteins |
| Fold Fold fold | a.25 — Ferritin-like |
| Superfamily Superfamily superfamily | a.25.1 — Ferritin-like |
| Family Family family | a.25.1.1 — Ferritin |
| Domain ID domain_id | 1aewA00 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 20 — Up-down Bundle |
| Topology topology | 1260 — Ferritin |
| Homologous superfamily homologous superfamily | 10 — Ferritin, core subunit, four-helix bundle |