Bacillus amyloliquefaciens
| 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 | T2BA_BACAM |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–213； UniProt 1–213 |
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 | 1bam |
| Deposition date deposition_date | 1994-12-28 |
| Structure title title | STRUCTURE OF RESTRICTION ENDONUCLEASE BAMHI PHASED AT 1.95 ANGSTROMS RESOLUTION BY MAD ANALYSIS |
| Keywords keywords | ENDONUCLEASE; ENDONUCLEASE |
| 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） | 25.54 Å |
| Rg (electron density) | 24.64 Å |
| Total Rg | 25.49 Å |
| Atom count | 3238 |
| Residues | 400 |
| Excluded volume | 58086 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1bama_ |
| Class class | c — Alpha and beta proteins (a/b) |
| Fold Fold fold | c.52 — Restriction endonuclease-like |
| Superfamily Superfamily superfamily | c.52.1 — Restriction endonuclease-like |
| Family Family family | c.52.1.3 — Restriction endonuclease BamHI |
| Domain ID domain_id | 1bamA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| Topology topology | 91 — Restriction Endonuclease |
| Homologous superfamily homologous superfamily | 20 — |