PYROCOCCUS HORIKOSHII
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | Protein 12 | COBALT (II) ION × 24 | Consistent with protein count |
| UniProt name | O58255_PYRHO |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–332； UniProt 1–332 |
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 | 2cf4 |
| Deposition date deposition_date | 2006-02-15 |
| Structure title title | Pyrococcus horikoshii TET1 peptidase can assemble into a tetrahedron or a large octahedral shell |
| Keywords keywords | AMINOPEPTIDASE, METALLOPROTEIN, HYPERTHERMOPHILE, ARCHAEA, TETRAHEDRAL, HYDROLASE; 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） | 48.84 Å |
| Rg (electron density) | 48.07 Å |
| Total Rg | 48.35 Å |
| Atom count | 31080 |
| Residues | 3924 |
| Excluded volume | 560880 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | 2cf4A01 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| Topology topology | 630 — Aminopeptidase |
| Homologous superfamily homologous superfamily | 10 — Zn peptidases |
| Domain ID domain_id | 2cf4A02 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 40 — Beta Barrel |
| Topology topology | 30 — Elongation Factor Tu (Ef-tu); domain 3 |
| Homologous superfamily homologous superfamily | 40 — Peptidase M42, domain 2 |