Saccharomyces cerevisiae
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | water × 1 | Consistent with protein count |
| UniProt name | STE5_YEAST |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 3–196； UniProt 593–786 |
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 | 3fze |
| Deposition date deposition_date | 2009-01-25 |
| Structure title title | Structure of the 'minimal scaffold' (ms) domain of Ste5 that cocatalyzes Fus3 phosphorylation by Ste7 |
| Keywords keywords | alpha/beta/alpha, vWA-like fold (SCOP), Cytoplasm, Pheromone response, Phosphoprotein, PROTEIN BINDING; PROTEIN BINDING |
| 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） | 17.16 Å |
| Rg (electron density) | 15.49 Å |
| Total Rg | 16.65 Å |
| Atom count | 1463 |
| Residues | 185 |
| Excluded volume | 26340 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | 3fzeA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| Topology topology | 50 — Rossmann fold |
| Homologous superfamily homologous superfamily | 11070 — Protein Ste5, Fus3-binding domain |