Homo sapiens
| 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 | PRIO_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–142； UniProt 90–231 |
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 | 1fkc |
| Deposition date deposition_date | 2000-08-09 |
| Structure title title | HUMAN PRION PROTEIN (MUTANT E200K) FRAGMENT 90-231 |
| Keywords keywords | three helix, CREUTZFELDT-JAKOB DISEASE, PRION, AGGREGATION, MEMBRANE PROTEIN; MEMBRANE PROTEIN |
| Experimental Method method | SOLUTION NMR |
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） | 16.14 Å |
| Rg (electron density) | 15.06 Å |
| Total Rg | 15.96 Å |
| Atom count | 1731 |
| Residues | 107 |
| Excluded volume | 15583 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1fkca_ |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.6 — Prion-like |
| Superfamily Superfamily superfamily | d.6.1 — Prion-like |
| Family Family family | d.6.1.1 — Prion-like |
| Domain ID domain_id | 1fkcA00 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 10 — Orthogonal Bundle |
| Topology topology | 790 — Major Prion Protein |
| Homologous superfamily homologous superfamily | 10 — Prion/Doppel protein, beta-ribbon domain |