CRITHIDIA FASCICULATA
| 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 | O96438 |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–146； UniProt 1–146 |
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 | 1o7u |
| Deposition date deposition_date | 2002-11-14 |
| Structure title title | Radiation induced tryparedoxin-I |
| Keywords keywords | ;TRYPAREDOXIN-I, SYNCHROTRON RADIATION, DISULFIDE BONDS TRYPAREDOXIN, CRITHIDIA FASCICULATA, THIOREDOXIN, TRYPANOSOME, ANOMALOUS DISPERSION, OXIDATIVE STRESS, OXIDOREDUCTASE, ELECTRON TRANSPORT ;; ELECTRON TRANSPORT |
| 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） | 15.74 Å |
| Rg (electron density) | 14.05 Å |
| Total Rg | 15.40 Å |
| Atom count | 1144 |
| Residues | 143 |
| Excluded volume | 20376 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1o7ua_ |
| 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.47.1.10 — Glutathione peroxidase-like |
| Domain ID domain_id | 1o7uA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| Topology topology | 30 — Glutaredoxin |
| Homologous superfamily homologous superfamily | 10 — Glutaredoxin |