OrganismNot specified
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | HEME C × 3 | Consistent with protein count |
| UniProt name | CYC3_DESAC |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–68； UniProt 1–68 |
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 | 1ehj |
| Deposition date deposition_date | 2000-02-21 |
| Structure title title | A PROTON-NMR INVESTIGATION OF THE FULLY REDUCED CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS |
| Keywords keywords | multi-heme, ELECTRON TRANSPORT; ELECTRON TRANSPORT |
| 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） | 12.99 Å |
| Rg (electron density) | 11.82 Å |
| Total Rg | 13.28 Å |
| Atom count | 1222 |
| Residues | 68 |
| Excluded volume | 11292 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1ehja_ |
| Class class | a — All alpha proteins |
| Fold Fold fold | a.138 — Multiheme cytochromes |
| Superfamily Superfamily superfamily | a.138.1 — Multiheme cytochromes |
| Family Family family | a.138.1.1 — Cytochrome c3-like |
| Domain ID domain_id | 1ehjA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 90 — Alpha-Beta Complex |
| Topology topology | 10 — Cytochrome C3 |
| Homologous superfamily homologous superfamily | 10 — Cytochrome C3 |