Bos taurus
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | CALCIUM ION × 1 water × 1 | Consistent with protein count |
| UniProt name | PA21B_BOVIN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 2–123； UniProt 24–145 |
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 | 3bp2 |
| Deposition date deposition_date | 1983-06-27 |
| Structure title title | ROLE OF THE N-TERMINUS IN THE INTERACTION OF PANCREATIC PHOSPHOLIPASE A2 WITH AGGREGATED SUBSTRATES. PROPERTIES AND CRYSTAL STRUCTURE OF TRANSAMINATED PHOSPHOLIPASE A2 |
| Keywords keywords | CARBOXYLIC ESTER HYDROLASE; CARBOXYLIC ESTER HYDROLASE |
| 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） | 15.35 Å |
| Rg (electron density) | 14.47 Å |
| Total Rg | 15.45 Å |
| Atom count | 958 |
| Residues | 122 |
| Excluded volume | 16771 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d3bp2a_ |
| Class class | a — All alpha proteins |
| Fold Fold fold | a.133 — Phospholipase A2, PLA2 |
| Superfamily Superfamily superfamily | a.133.1 — Phospholipase A2, PLA2 |
| Family Family family | a.133.1.2 — Vertebrate phospholipase A2 |
| Domain ID domain_id | 3bp2A00 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 20 — Up-down Bundle |
| Topology topology | 90 — Phospholipase A2 |
| Homologous superfamily homologous superfamily | 10 — Phospholipase A2 domain |