STREPTOMYCES SP. 11AG8
| 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 | Q9KIH1 |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–222； UniProt 32–253 |
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 | 1oa4 |
| Deposition date deposition_date | 2002-12-28 |
| Structure title title | Comparison of Family 12 Glycoside Hydrolases and Recruited Substitutions Important for Thermal Stability |
| Keywords keywords | HYDROLASE, CELLULASE, CELLULOSE DEGRADATION, ENDOGLUCANASE, GLYCOSYL HYDROLASE, GH FAMILY 12, STREPTOMYCES SP 11AG8 CEL12A; HYDROLASE |
| 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） | 17.11 Å |
| Rg (electron density) | 15.80 Å |
| Total Rg | 16.88 Å |
| Atom count | 1685 |
| Residues | 222 |
| Excluded volume | 29344 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1oa4a_ |
| Class class | b — All beta proteins |
| Fold Fold fold | b.29 — Concanavalin A-like lectins/glucanases |
| Superfamily Superfamily superfamily | b.29.1 — Concanavalin A-like lectins/glucanases |
| Family Family family | b.29.1.11 — Xylanase/endoglucanase 11/12 |
| Domain ID domain_id | 1oa4A00 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 60 — Sandwich |
| Topology topology | 120 — Jelly Rolls |
| Homologous superfamily homologous superfamily | 180 — Glycoside hydrolase family 11/12, catalytic domain |