Locusta migratoria
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | No other associated polymer | Consistent with protein count |
| UniProt name | APL3_LOCMI |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–161； UniProt 20–180 |
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 | 1aep |
| Deposition date deposition_date | 1992-11-30 |
| Structure title title | MOLECULAR STRUCTURE OF AN APOLIPOPROTEIN DETERMINED AT 2.5-ANGSTROMS RESOLUTION |
| Keywords keywords | LIPOPROTEIN; LIPOPROTEIN |
| 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） | 17.46 Å |
| Rg (electron density) | 16.61 Å |
| Total Rg | 17.48 Å |
| Atom count | 1161 |
| Residues | 153 |
| Excluded volume | 20263 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1aepa_ |
| Class class | a — All alpha proteins |
| Fold Fold fold | a.63 — Apolipophorin-III |
| Superfamily Superfamily superfamily | a.63.1 — Apolipophorin-III |
| Family Family family | a.63.1.1 — Apolipophorin-III |
| Domain ID domain_id | 1aepA00 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 20 — Up-down Bundle |
| Topology topology | 120 — Four Helix Bundle (Hemerythrin (Met), subunit A) |
| Homologous superfamily homologous superfamily | 20 — Apolipoprotein |