RATTUS NORVEGICUS
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | Protein 2 | No other associated polymer | Consistent with protein count |
| UniProt name | SH3G2_RAT |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 62–204； UniProt 1–143 |
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 | 2c08 |
| Deposition date deposition_date | 2005-08-26 |
| Structure title title | Rat endophilin A1 BAR domain |
| Keywords keywords | ;ENDOCYTOSIS, BAR DOMAIN, MEMBRANE CURVATURE, SH3 DOMAIN, ACYLTRANSFERASE, COILED COIL, LIPID-BINDING, MULTIGENE FAMILY, PHOSPHORYLATION, 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） | 32.89 Å |
| Rg (electron density) | 33.95 Å |
| Total Rg | 33.54 Å |
| Atom count | 3306 |
| Residues | 392 |
| Excluded volume | 58898 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d2c08a1 |
| Class class | a — All alpha proteins |
| Fold Fold fold | a.238 — BAR/IMD domain-like |
| Superfamily Superfamily superfamily | a.238.1 — BAR/IMD domain-like |
| Family Family family | a.238.1.1 — BAR domain |
| Domain ID domain_id | 2c08A00 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 20 — Up-down Bundle |
| Topology topology | 1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2 |
| Homologous superfamily homologous superfamily | 60 — Arfaptin homology (AH) domain/BAR domain |