Homo sapiens
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | Protein 2 | GLYCEROL × 2 CHLORIDE ION × 2 water × 2 | Consistent with protein count |
| UniProt name | SDOS_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 2–207； UniProt 6–211 |
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 | 3kvh |
| Deposition date deposition_date | 2009-11-30 |
| Structure title title | Crystal structure of human protein syndesmos (NUDT16-like protein) |
| Keywords keywords | ;NUDT16-LIKE, NUDT16L1, SYNDESMOS, NUDIX, RNA REGULATION, RNA-BINDING, STRUCTURAL GENOMICS CONSORTIUM, SGC, RNA DEGRADATION, RNA BINDING PROTEIN ;; RNA BINDING PROTEIN |
| 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） | 22.51 Å |
| Rg (electron density) | 21.28 Å |
| Total Rg | 22.21 Å |
| Atom count | 3026 |
| Residues | 384 |
| Excluded volume | 54464 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d3kvha_ |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.113 — Nudix |
| Superfamily Superfamily superfamily | d.113.1 — Nudix |
| Family Family family | d.113.1.0 — automated matches |
| Domain ID domain_id | 3kvhA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 90 — Alpha-Beta Complex |
| Topology topology | 79 — Nucleoside Triphosphate Pyrophosphohydrolase |
| Homologous superfamily homologous superfamily | 10 — Nucleoside Triphosphate Pyrophosphohydrolase |