ESCHERICHIA COLI
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | Protein 3 | DECANE × 6 HEXANE × 3 water × 3 | Consistent with protein count |
| UniProt name | OMPC_ECOL6 |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–354； UniProt 22–375 |
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 | 2xe1 |
| Deposition date deposition_date | 2010-05-10 |
| Structure title title | Molecular insights into clinically isolated OmpC mutants and their role in multi-drug resistance |
| Keywords keywords | TRANSPORT PROTEIN, ION TRANSPORT, PORIN, ANTIBIOTIC RESISTANCE, CELL OUTER MEMBRANE, BETA BARREL, MEMBRANE PROTEIN; TRANSPORT PROTEIN |
| 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） | 30.91 Å |
| Rg (electron density) | 30.43 Å |
| Total Rg | 31.20 Å |
| Atom count | 8403 |
| Residues | 1062 |
| Excluded volume | 146720 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d2xe1a_ |
| Class class | f — Membrane and cell surface proteins and peptides |
| Fold Fold fold | f.4 — Transmembrane beta-barrels |
| Superfamily Superfamily superfamily | f.4.3 — Porins |
| Family Family family | f.4.3.1 — Porin |
| Domain ID domain_id | 2xe1A00 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 40 — Beta Barrel |
| Topology topology | 160 — Porin |
| Homologous superfamily homologous superfamily | 10 — Porin |