Piromyces equi
| 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 | Q9P868_PIREQ |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–46； UniProt 20–65 |
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 | 1e8p |
| Deposition date deposition_date | 2000-09-28 |
| Structure title title | Characterisation of the cellulose docking domain from Piromyces equi |
| Keywords keywords | CELLULOSE DOCKING DOMAIN, CELLULASE; CELLULOSE DOCKING DOMAIN |
| 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） | 10.67 Å |
| Rg (electron density) | 9.33 Å |
| Total Rg | 10.77 Å |
| Atom count | 649 |
| Residues | 46 |
| Excluded volume | 5981 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1e8pa_ |
| Class class | g — Small proteins |
| Fold Fold fold | g.55 — Cellulose docking domain, dockering |
| Superfamily Superfamily superfamily | g.55.1 — Cellulose docking domain, dockering |
| Family Family family | g.55.1.1 — Cellulose docking domain, dockering |
| Domain ID domain_id | 1e8pA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 90 — Alpha-Beta Complex |
| Topology topology | 1220 — Endoglucanase; Chain: A |
| Homologous superfamily homologous superfamily | 10 — Cellulose docking domain, dockering |