Homo sapiens
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | SODIUM ION × 1 water × 1 | Consistent with protein count |
| UniProt name | LYSC_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–130； UniProt 19–148 |
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 | 1ouh |
| Deposition date deposition_date | 1996-08-23 |
| Structure title title | CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V74A MUTANT |
| Keywords keywords | HYDROLASE (O-GLYCOSYL), AMYLOID, DISEASE MUTATION; HYDROLASE (O-GLYCOSYL) |
| 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） | 15.47 Å |
| Rg (electron density) | 14.13 Å |
| Total Rg | 15.25 Å |
| Atom count | 1028 |
| Residues | 130 |
| Excluded volume | 17959 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1ouha_ |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.2 — Lysozyme-like |
| Superfamily Superfamily superfamily | d.2.1 — Lysozyme-like |
| Family Family family | d.2.1.2 — C-type lysozyme |
| Domain ID domain_id | 1ouhA00 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 10 — Orthogonal Bundle |
| Topology topology | 530 — Lysozyme |
| Homologous superfamily homologous superfamily | 10 — |