CAENORHABDITIS ELEGANS
| 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 | CYP3_CAEEL |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–173； UniProt 1–173 |
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 | 1dyw |
| Deposition date deposition_date | 2000-02-10 |
| Structure title title | Biochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegans |
| Keywords keywords | ISOMERASE(PEPTIDYL-PROLYL CIS-TRANS), ISOMERASE, ROTAMASE; ISOMERASE(PEPTIDYL-PROLYL CIS-TRANS) |
| 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） | 15.61 Å |
| Rg (electron density) | 14.46 Å |
| Total Rg | 15.67 Å |
| Atom count | 1296 |
| Residues | 172 |
| Excluded volume | 23007 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1dywa_ |
| Class class | b — All beta proteins |
| Fold Fold fold | b.62 — Cyclophilin-like |
| Superfamily Superfamily superfamily | b.62.1 — Cyclophilin-like |
| Family Family family | b.62.1.1 — Cyclophilin (peptidylprolyl isomerase) |
| Domain ID domain_id | 1dywA00 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 40 — Beta Barrel |
| Topology topology | 100 — Cyclophilin |
| Homologous superfamily homologous superfamily | 10 — Cyclophilin-like |