MUS MUSCULUS
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | Protein 2 | COBALT (II) ION × 2 water × 2 | Consistent with protein count |
| UniProt name | RIR2_MOUSE |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–390； UniProt 1–390 |
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 | 1h0o |
| Deposition date deposition_date | 2002-06-26 |
| Structure title title | Cobalt substitution of mouse R2 ribonucleotide reductase to model the reactive diferrous state |
| Keywords keywords | OXIDOREDUCTASE, RIBONUCLEOTIDE REDUCTASE, DINUCLEAR METAL-CLUSTER; OXIDOREDUCTASE |
| 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） | 26.48 Å |
| Rg (electron density) | 25.69 Å |
| Total Rg | 26.62 Å |
| Atom count | 4762 |
| Residues | 576 |
| Excluded volume | 85231 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1h0oa_ |
| Class class | a — All alpha proteins |
| Fold Fold fold | a.25 — Ferritin-like |
| Superfamily Superfamily superfamily | a.25.1 — Ferritin-like |
| Family Family family | a.25.1.2 — Ribonucleotide reductase-like |
| Domain ID domain_id | 1h0oA00 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 10 — Orthogonal Bundle |
| Topology topology | 620 — Ribonucleotide Reductase, subunit A |
| Homologous superfamily homologous superfamily | 20 — Ribonucleotide Reductase, subunit A |