Streptomyces sp.
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | SODIUM ION × 1 water × 1 | Consistent with protein count |
| UniProt name | DACX_STRSK |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–262； UniProt 30–291 |
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 | 1es3 |
| Deposition date deposition_date | 2000-04-07 |
| Structure title title | C98A mutant of streptomyces K15 DD-transpeptidase |
| Keywords keywords | PENICILLIN-BINDING, DD-TRANSPEPTIDASE, SERINE PEPTIDASE, BETA-LACTAMASE, HYDROLASE CARBOXYPEPTIDASE, 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） | 18.66 Å |
| Rg (electron density) | 17.69 Å |
| Total Rg | 18.63 Å |
| Atom count | 1913 |
| Residues | 260 |
| Excluded volume | 34171 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1es3a_ |
| Class class | e — Multi-domain proteins (alpha and beta) |
| Fold Fold fold | e.3 — beta-lactamase/transpeptidase-like |
| Superfamily Superfamily superfamily | e.3.1 — beta-lactamase/transpeptidase-like |
| Family Family family | e.3.1.1 — beta-Lactamase/D-ala carboxypeptidase |
| Domain ID domain_id | 1es3A00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| Topology topology | 710 — Beta-lactamase |
| Homologous superfamily homologous superfamily | 10 — DD-peptidase/beta-lactamase superfamily |