Escherichia coli
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | Protein 2 | water × 2 | Consistent with protein count |
| UniProt name | ROP_ECOLI |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–63； UniProt 1–63 |
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 | 1rop |
| Deposition date deposition_date | 1991-04-02 |
| Structure title title | STRUCTURE OF THE COL*E1 ROP PROTEIN AT 1.7 ANGSTROMS RESOLUTION |
| Keywords keywords | TRANSCRIPTION REGULATION; TRANSCRIPTION REGULATION |
| 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） | 15.35 Å |
| Rg (electron density) | 14.38 Å |
| Total Rg | 15.37 Å |
| Atom count | 894 |
| Residues | 112 |
| Excluded volume | 15661 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1ropa_ |
| Class class | a — All alpha proteins |
| Fold Fold fold | a.30 — ROP-like |
| Superfamily Superfamily superfamily | a.30.1 — ROP protein |
| Family Family family | a.30.1.1 — ROP protein |
| Domain ID domain_id | 1ropA00 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 10 — Orthogonal Bundle |
| Topology topology | 287 — Helix Hairpins |
| Homologous superfamily homologous superfamily | 230 — |