Escherichia coli
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | Protein 2 | No other associated polymer | Consistent with protein count |
| UniProt name | IDH_ECOLI |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–416； UniProt 1–416 |
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 | 1idd |
| Deposition date deposition_date | 1995-01-18 |
| Structure title title | ISOCITRATE DEHYDROGENASE Y160F MUTANT APO ENZYME |
| Keywords keywords | OXIDOREDUCTASE (NAD(A)-CHOH(D)); OXIDOREDUCTASE (NAD(A)-CHOH(D)) |
| 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） | 29.01 Å |
| Rg (electron density) | 28.05 Å |
| Total Rg | 28.90 Å |
| Atom count | 6434 |
| Residues | 828 |
| Excluded volume | 114630 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1idda_ |
| Class class | c — Alpha and beta proteins (a/b) |
| Fold Fold fold | c.77 — Isocitrate/Isopropylmalate dehydrogenase-like |
| Superfamily Superfamily superfamily | c.77.1 — Isocitrate/Isopropylmalate dehydrogenase-like |
| Family Family family | c.77.1.1 — Dimeric isocitrate & isopropylmalate dehydrogenases |
| Domain ID domain_id | 1iddA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| Topology topology | 718 — Isopropylmalate Dehydrogenase |
| Homologous superfamily homologous superfamily | 10 — Isopropylmalate Dehydrogenase |