Homo sapiens
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | Canertinib × 1 water × 1 | Consistent with protein count |
| UniProt name | EGFR_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–327； UniProt 696–1022 |
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 | 9os6 |
| Deposition date deposition_date | 2025-05-23 |
| Structure title title | Canertinib (CI-1033) in complex with wild-type EGFR |
| Keywords keywords | Cancer, Drug Discovery, Covalent, TRANSFERASE; TRANSFERASE |
| 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） | 20.39 Å |
| Rg (electron density) | 19.49 Å |
| Total Rg | 20.52 Å |
| Atom count | 2236 |
| Residues | 277 |
| Excluded volume | 40331 ų |
| Maximum q | 0.500 Å⁻¹ |