Synechococcus sp.
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | Protein 2 | water × 2 | Consistent with protein count |
| UniProt name | Q44177_SYNP2 |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–134； UniProt 1–134 |
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 | 2z44 |
| Deposition date deposition_date | 2007-06-12 |
| Structure title title | Crystal Structure of Selenomethionine-labeled ORF134 |
| Keywords keywords | chaperone, helix bundle; CHAPERONE |
| 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） | 21.14 Å |
| Rg (electron density) | 20.28 Å |
| Total Rg | 21.06 Å |
| Atom count | 1790 |
| Residues | 214 |
| Excluded volume | 32226 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d2z44a_ |
| Class class | a — All alpha proteins |
| Fold Fold fold | a.280 — RbcX-like |
| Superfamily Superfamily superfamily | a.280.1 — RbcX-like |
| Family Family family | a.280.1.1 — RbcX-like |
| Domain ID domain_id | 2z44A00 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 10 — Orthogonal Bundle |
| Topology topology | 1200 — Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein; Chain A |
| Homologous superfamily homologous superfamily | 210 — Chaperonin-like RbcX |