Escherichia coli
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | No other associated polymer | Consistent with protein count |
| UniProt name | DSBA_ECOLI |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–189； UniProt 20–208 |
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 | 1a23 |
| Deposition date deposition_date | 1998-01-15 |
| Structure title title | SOLUTION NMR STRUCTURE OF REDUCED DSBA FROM ESCHERICHIA COLI, MINIMIZED AVERAGE STRUCTURE |
| Keywords keywords | THIOL-DISULFIDE OXIDOREDUCTASE, INTRODUCTION OF DISULFIDE BONDS, PROTEIN FOLDING, REDOX-ACTIVE CENTER, OXIDOREDUCTASE; OXIDOREDUCTASE |
| Experimental Method method | SOLUTION NMR |
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） | 18.22 Å |
| Rg (electron density) | 17.00 Å |
| Total Rg | 18.10 Å |
| Atom count | 2952 |
| Residues | 189 |
| Excluded volume | 26571 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1a23a_ |
| Class class | c — Alpha and beta proteins (a/b) |
| Fold Fold fold | c.47 — Thioredoxin fold |
| Superfamily Superfamily superfamily | c.47.1 — Thioredoxin-like |
| Family Family family | c.47.1.13 — DsbA-like |
| Domain ID domain_id | 1a23A00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| Topology topology | 30 — Glutaredoxin |
| Homologous superfamily homologous superfamily | 10 — Glutaredoxin |