Escherichia coli
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | water × 1 | Consistent with protein count |
| UniProt name | BLT1_ECOLX |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 2–261； UniProt 32–291 |
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 | 6c78 |
| Deposition date deposition_date | 2018-01-22 |
| Structure title title | Substrate Binding Induces Conformational Changes In A Class A Beta Lactamase That Primes It For Catalysis |
| Keywords keywords | HYDROLASE; HYDROLASE |
| Experimental Method method | NEUTRON 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） | 19.83 Å |
| Rg (electron density) | 17.77 Å |
| Total Rg | 19.43 Å |
| Atom count | 4200 |
| Residues | 259 |
| Excluded volume | 47529 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d6c78a_ |
| 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 | 6c78A00 |
| 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 |