Actinidia chinensis
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | AMMONIUM ION × 1 water × 1 | Consistent with protein count |
| UniProt name | ACTN_ACTCH |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–220； UniProt 127–346 |
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 | 2act |
| Deposition date deposition_date | 1979-11-27 |
| Structure title title | CRYSTALLOGRAPHIC REFINEMENT OF THE STRUCTURE OF ACTINIDIN AT 1.7 ANGSTROMS RESOLUTION BY FAST FOURIER LEAST-SQUARES METHODS |
| Keywords keywords | HYDROLASE (PROTEINASE); HYDROLASE (PROTEINASE) |
| 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） | 17.46 Å |
| Rg (electron density) | 16.22 Å |
| Total Rg | 17.22 Å |
| Atom count | 1648 |
| Residues | 217 |
| Excluded volume | 28914 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d2acta_ |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.3 — Cysteine proteinases |
| Superfamily Superfamily superfamily | d.3.1 — Cysteine proteinases |
| Family Family family | d.3.1.1 — Papain-like |
| Domain ID domain_id | 2actA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 90 — Alpha-Beta Complex |
| Topology topology | 70 — Cathepsin B; Chain A |
| Homologous superfamily homologous superfamily | 10 — Cysteine proteinases |