Mus musculus
| 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 | ADRM1_MOUSE |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 5–153； UniProt 2–150 |
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 | 2r2y |
| Deposition date deposition_date | 2007-08-28 |
| Structure title title | Crystal structure of the proteasomal Rpn13 PRU-domain |
| Keywords keywords | ;proteasome, ubiquitin, PH-domain, 19S regulator, receptor, UBIQUITIN-PROTEASOME-DEGRADATION PATHWAY, RECEPTOR DOMAIN FOR UBIQUITIN AND PROTEASOME BINDING, 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） | 14.90 Å |
| Rg (electron density) | 13.49 Å |
| Total Rg | 14.84 Å |
| Atom count | 895 |
| Residues | 109 |
| Excluded volume | 15915 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | 2r2yA00 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 30 — Roll |
| Topology topology | 29 — PH-domain like |
| Homologous superfamily homologous superfamily | 70 — Proteasomal ubiquitin receptor Rpn13/ADRM1 |