Thermoplasma acidophilum
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | Protein 2 | SODIUM ION × 2 PHOSPHATE ION × 6 water × 2 | Consistent with protein count |
| UniProt name | THSA_THEAC |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 2–153； UniProt 214–365 |
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 | 1ass |
| Deposition date deposition_date | 1997-08-11 |
| Structure title title | APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM |
| Keywords keywords | CHAPERONIN, HSP60, THERMOSOME, TCP1, GROEL, THERMOPLASMA ACIDOPHILUM, ATP-BINDING; CHAPERONIN |
| 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） | 26.68 Å |
| Rg (electron density) | 26.76 Å |
| Total Rg | 27.49 Å |
| Atom count | 2382 |
| Residues | 304 |
| Excluded volume | 42844 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1assa_ |
| Class class | c — Alpha and beta proteins (a/b) |
| Fold Fold fold | c.8 — The 'swivelling' beta/beta/alpha domain |
| Superfamily Superfamily superfamily | c.8.5 — GroEL apical domain-like |
| Family Family family | c.8.5.2 — Group II chaperonin (CCT, TRIC), apical domain |
| Domain ID domain_id | 1assA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 50 — 3-Layer(bba) Sandwich |
| Topology topology | 7 — GroEL |
| Homologous superfamily homologous superfamily | 10 — GroEL |