Homo sapiens
| 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 | TP4A3_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–173； UniProt 1–173 |
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 | 1v3a |
| Deposition date deposition_date | 2003-10-30 |
| Structure title title | Structure of human PRL-3, the phosphatase associated with cancer metastasis |
| Keywords keywords | hydrolase; HYDROLASE |
| 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） | 17.59 Å |
| Rg (electron density) | 16.10 Å |
| Total Rg | 17.38 Å |
| Atom count | 2594 |
| Residues | 162 |
| Excluded volume | 23066 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1v3aa_ |
| Class class | c — Alpha and beta proteins (a/b) |
| Fold Fold fold | c.45 — (Phosphotyrosine protein) phosphatases II |
| Superfamily Superfamily superfamily | c.45.1 — (Phosphotyrosine protein) phosphatases II |
| Family Family family | c.45.1.1 — Dual specificity phosphatase-like |
| Domain ID domain_id | 1v3aA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 90 — Alpha-Beta Complex |
| Topology topology | 190 — Protein-Tyrosine Phosphatase; Chain A |
| Homologous superfamily homologous superfamily | 10 — Protein tyrosine phosphatase superfamily |