Bacillus sp.
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | Protein 6 | PROPIONAMIDE × 6 CHLORIDE ION × 6 water × 6 | Consistent with protein count |
| UniProt name | AMIE_BACSP |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–348； UniProt 1–348 |
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 | 4gyl |
| Deposition date deposition_date | 2012-09-05 |
| Structure title title | The E142L mutant of the amidase from Geobacillus pallidus showing the result of Michael addition of acrylamide at the active site cysteine |
| Keywords keywords | amidase, catalytic tetrad, amidase mechanism, acrylamide, Michael Adduct, 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） | 34.86 Å |
| Rg (electron density) | 33.84 Å |
| Total Rg | 34.42 Å |
| Atom count | 15930 |
| Residues | 2040 |
| Excluded volume | 282760 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | 4gylA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 60 — 4-Layer Sandwich |
| Topology topology | 110 — Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase |
| Homologous superfamily homologous superfamily | 10 — Carbon-nitrogen hydrolase |