Proteus vulgaris
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | CHLORIDE ION × 4 water × 1 | Consistent with protein count |
| UniProt name | Q7A225_PROVU |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 3–93； UniProt 2–92 |
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 | 4px8 |
| Deposition date deposition_date | 2014-03-22 |
| Structure title title | Structure of P. vulgaris HigB toxin |
| Keywords keywords | ;BACTERIAL TOXINS, BIOFILMS, CELL METABOLISM, ENERGY METABOLISM, MICROBIAL PATHOGENESIS, STRESS RESPONSE, STRINGENT RESPONSE, TRANSLATION CONTROL, TOXIN, MICROBIAL RNASE FOLD, RIBOSOME-DEPENDENT mRNA INTERFERASE, HOST INHIBITION OF GROWTH A, mRNA, AND RIBOSOME ;; TOXIN |
| 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） | 14.25 Å |
| Rg (electron density) | 12.77 Å |
| Total Rg | 14.22 Å |
| Atom count | 815 |
| Residues | 99 |
| Excluded volume | 14507 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | 4px8A00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 2310 — YaeB-like fold |
| Homologous superfamily homologous superfamily | 20 — RelE-like |