Mus musculus
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | Protein 2 | water × 2 | Consistent with protein count |
| UniProt name | EPHA4_MOUSE |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–94； UniProt 888–981 |
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 | 1b0x |
| Deposition date deposition_date | 1998-11-14 |
| Structure title title | THE CRYSTAL STRUCTURE OF AN EPH RECEPTOR SAM DOMAIN REVEALS A MECHANISM FOR MODULAR DIMERIZATION. |
| Keywords keywords | RECEPTOR TYROSINE KINASE, PROTEIN INTERACTION MODULE, DIMERIZATION DOMAIN, TRANSFERASE; TRANSFERASE |
| 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） | 18.11 Å |
| Rg (electron density) | 17.49 Å |
| Total Rg | 18.19 Å |
| Atom count | 1390 |
| Residues | 144 |
| Excluded volume | 19894 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1b0xa_ |
| Class class | a — All alpha proteins |
| Fold Fold fold | a.60 — SAM domain-like |
| Superfamily Superfamily superfamily | a.60.1 — SAM/Pointed domain |
| Family Family family | a.60.1.2 — SAM (sterile alpha motif) domain |
| Domain ID domain_id | 1b0xA00 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 10 — Orthogonal Bundle |
| Topology topology | 150 — DNA polymerase; domain 1 |
| Homologous superfamily homologous superfamily | 50 — Transcription Factor, Ets-1 |