Human immunodeficiency virus 1
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | Protein 2 | GLYCEROL × 4 water × 2 | Consistent with protein count |
| UniProt name | Q8ALR4_9HIV1 |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–99； UniProt 1–99 |
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 | 2r8n |
| Deposition date deposition_date | 2007-09-11 |
| Structure title title | Structural Analysis of the Unbound Form of HIV-1 Subtype C Protease |
| Keywords keywords | ;HIV-1 subtype C, Aspartyl protease, Hydrolase, Multifunctional enzyme, Nucleotidyltransferase, Protease, RNA-directed DNA polymerase, Transferase ;; HYDROLASE |
| 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） | 18.80 Å |
| Rg (electron density) | 17.94 Å |
| Total Rg | 18.92 Å |
| Atom count | 1532 |
| Residues | 198 |
| Excluded volume | 28134 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d2r8na_ |
| Class class | b — All beta proteins |
| Fold Fold fold | b.50 — Acid proteases |
| Superfamily Superfamily superfamily | b.50.1 — Acid proteases |
| Family Family family | b.50.1.1 — Retroviral protease (retropepsin) |
| Domain ID domain_id | 2r8nA00 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 40 — Beta Barrel |
| Topology topology | 70 — Cathepsin D, subunit A; domain 1 |
| Homologous superfamily homologous superfamily | 10 — Acid Proteases |