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 | LEXA_ECOLI |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–135； UniProt 68–202 |
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 | 1jhc |
| Deposition date deposition_date | 2001-06-27 |
| Structure title title | LEXA S119A C-TERMINAL TRYPTIC FRAGMENT |
| Keywords keywords | LexA SOS repressor, HYDROLASE; 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） | 21.31 Å |
| Rg (electron density) | 20.23 Å |
| Total Rg | 21.08 Å |
| Atom count | 2012 |
| Residues | 260 |
| Excluded volume | 36094 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1jhca_ |
| Class class | b — All beta proteins |
| Fold Fold fold | b.87 — LexA/Signal peptidase |
| Superfamily Superfamily superfamily | b.87.1 — LexA/Signal peptidase |
| Family Family family | b.87.1.1 — LexA-related |
| Domain ID domain_id | 1jhcA00 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 10 — Ribbon |
| Topology topology | 109 — Umud Fragment, subunit A |
| Homologous superfamily homologous superfamily | 10 — Umud Fragment, subunit A |