Ascaris suum
| 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 | ITR1_ASCSU |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–62； UniProt 1–62 |
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 | 1ata |
| Deposition date deposition_date | 1994-05-20 |
| Structure title title | HIGH-RESOLUTION STRUCTURE OF ASCARIS TRYPSIN INHIBITOR IN SOLUTION: DIRECT EVIDENCE FOR A PH INDUCED CONFORMATIONAL TRANSITION IN THE REACTIVE SITE |
| Keywords keywords | PROTEINASE INHIBITOR(TRYPSIN); PROTEINASE INHIBITOR(TRYPSIN) |
| 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） | 12.94 Å |
| Rg (electron density) | 12.00 Å |
| Total Rg | 13.30 Å |
| Atom count | 912 |
| Residues | 62 |
| Excluded volume | 8214 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1ataa_ |
| Class class | g — Small proteins |
| Fold Fold fold | g.22 — Serine protease inhibitors |
| Superfamily Superfamily superfamily | g.22.1 — Serine protease inhibitors |
| Family Family family | g.22.1.1 — ATI-like |
| Domain ID domain_id | 1ataA00 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 10 — Ribbon |
| Topology topology | 25 — Laminin |
| Homologous superfamily homologous superfamily | 10 — Laminin |