Escherichia coli
| 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 | ZIPA_ECOLI |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–144； UniProt 185–328 |
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 | 1f7w |
| Deposition date deposition_date | 2000-06-28 |
| Structure title title | SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA |
| Keywords keywords | Alpha-Beta fold, CELL DIVISION, SEPTATION, TRANSMEMBRANE, CELL CYCLE; CELL CYCLE |
| 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） | 16.47 Å |
| Rg (electron density) | 15.13 Å |
| Total Rg | 16.25 Å |
| Atom count | 2246 |
| Residues | 144 |
| Excluded volume | 20058 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1f7wa_ |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.129 — TBP-like |
| Superfamily Superfamily superfamily | d.129.4 — Cell-division protein ZipA, C-terminal domain |
| Family Family family | d.129.4.1 — Cell-division protein ZipA, C-terminal domain |
| Domain ID domain_id | 1f7wA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 1400 — Cell Division Protein Zipa; Chain: A, |
| Homologous superfamily homologous superfamily | 10 — ZipA, C-terminal FtsZ-binding domain |