Escherichia coli
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | Protein 3 | water × 3 | Consistent with protein count |
| UniProt name | LPP_ECOLI |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–56； UniProt 22–77 |
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 | 1kfm |
| Deposition date deposition_date | 2001-11-21 |
| Structure title title | Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants |
| Keywords keywords | LIPOPROTEIN, PROTEIN FOLDING, HELIX CAPPING, ALANINE-ZIPPER, MEMBRANE PROTEIN; MEMBRANE 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） | 21.72 Å |
| Rg (electron density) | 22.13 Å |
| Total Rg | 22.74 Å |
| Atom count | 1089 |
| Residues | 150 |
| Excluded volume | 18694 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1kfma_ |
| Class class | h — Coiled coil proteins |
| Fold Fold fold | h.1 — Parallel coiled-coil |
| Superfamily Superfamily superfamily | h.1.16 — Outer membrane lipoprotein |
| Family Family family | h.1.16.1 — Outer membrane lipoprotein |
| Domain ID domain_id | 1kfmA00 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 20 — Up-down Bundle |
| Topology topology | 5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces |
| Homologous superfamily homologous superfamily | 190 — |