Escherichia coli
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | Protein 4 | water × 4 | Consistent with protein count |
| UniProt name | DYR21_ECOLI |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–62； UniProt 17–78 |
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 | 1vie |
| Deposition date deposition_date | 1996-10-03 |
| Structure title title | STRUCTURE OF DIHYDROFOLATE REDUCTASE |
| Keywords keywords | OXIDOREDUCTASE, NADP, TRIMETHOPRIM RESISTANCE, METHOTREXATE RESISTANCE, ONE-CARBON METABOLISM, PLASMID; OXIDOREDUCTASE |
| 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） | 19.27 Å |
| Rg (electron density) | 17.80 Å |
| Total Rg | 18.88 Å |
| Atom count | 1828 |
| Residues | 240 |
| Excluded volume | 32083 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1viea_ |
| Class class | b — All beta proteins |
| Fold Fold fold | b.34 — SH3-like barrel |
| Superfamily Superfamily superfamily | b.34.4 — Electron transport accessory proteins |
| Family Family family | b.34.4.1 — R67 dihydrofolate reductase |
| Domain ID domain_id | 1vieA00 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 30 — Roll |
| Topology topology | 30 — SH3 type barrels. |
| Homologous superfamily homologous superfamily | 60 — |