Thermus thermophilus
| 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 | RPOA_THETH |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–69； UniProt 247–315 |
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 | 1doq |
| Deposition date deposition_date | 1999-12-21 |
| Structure title title | THE C-TERMINAL DOMAIN OF THE RNA POLYMERASE ALPHA SUBUNIT FROM THERMUS THERMOPHILUS |
| Keywords keywords | TRANSCRIPTION, RNA POLYMERASE, THERMUS THERMOPHILUS, TRANSFERASE; TRANSFERASE |
| Experimental Method method | SOLUTION NMR |
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） | 13.08 Å |
| Rg (electron density) | 11.17 Å |
| Total Rg | 12.75 Å |
| Atom count | 1118 |
| Residues | 69 |
| Excluded volume | 9855 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1doqa_ |
| Class class | a — All alpha proteins |
| Fold Fold fold | a.60 — SAM domain-like |
| Superfamily Superfamily superfamily | a.60.3 — C-terminal domain of RNA polymerase alpha subunit |
| Family Family family | a.60.3.1 — C-terminal domain of RNA polymerase alpha subunit |
| Domain ID domain_id | 1doqA00 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 10 — Orthogonal Bundle |
| Topology topology | 150 — DNA polymerase; domain 1 |
| Homologous superfamily homologous superfamily | 20 — 5' to 3' exonuclease, C-terminal subdomain |