Thermoplasma acidophilum
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | LEUCINE × 1 water × 1 | Consistent with protein count |
| UniProt name | PIP_THEAC |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–293； UniProt 1–293 |
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 | 1xro |
| Deposition date deposition_date | 2004-10-15 |
| Structure title title | Crystal structure of active site F1-mutant E213Q soaked with peptide Phe-Leu |
| Keywords keywords | ALPHA-BETA HYDROLASE, CAGED ACTIVE SITE, SUBSTRATE RECOGNITION, HYDROGEN BONDED NETWORK, PEPTIDE CLEAVAGE, hydrolase; 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） | 19.30 Å |
| Rg (electron density) | 18.15 Å |
| Total Rg | 19.09 Å |
| Atom count | 2341 |
| Residues | 290 |
| Excluded volume | 41775 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1xroa_ |
| Class class | c — Alpha and beta proteins (a/b) |
| Fold Fold fold | c.69 — alpha/beta-Hydrolases |
| Superfamily Superfamily superfamily | c.69.1 — alpha/beta-Hydrolases |
| Family Family family | c.69.1.7 — Proline iminopeptidase-like |
| Domain ID domain_id | 1xroA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| Topology topology | 50 — Rossmann fold |
| Homologous superfamily homologous superfamily | 1820 — Alpha/Beta hydrolase fold, catalytic domain |