Bos taurus
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | No other associated polymer | Consistent with protein count |
| UniProt name | RNAS1_BOVIN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–124； UniProt 27–150 |
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 | 9rat |
| Deposition date deposition_date | 1991-08-13 |
| Structure title title | EFFECTS OF TEMPERATURE ON PROTEIN STRUCTURE AND DYNAMICS: X-RAY CRYSTALLOGRAPHIC STUDIES OF THE PROTEIN RIBONUCLEASE-A AT NINE DIFFERENT TEMPERATURES FROM 98 TO 320 K |
| Keywords keywords | HYDROLASE (NUCLEIC ACID, RNA); HYDROLASE (NUCLEIC ACID,RNA) |
| 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） | 15.23 Å |
| Rg (electron density) | 14.31 Å |
| Total Rg | 15.31 Å |
| Atom count | 951 |
| Residues | 124 |
| Excluded volume | 16587 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d9rata_ |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.5 — RNase A-like |
| Superfamily Superfamily superfamily | d.5.1 — RNase A-like |
| Family Family family | d.5.1.1 — Ribonuclease A-like |
| Domain ID domain_id | 9ratA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 10 — Roll |
| Topology topology | 130 — P-30 Protein |
| Homologous superfamily homologous superfamily | 10 — Ribonuclease A-like domain |