Escherichia coli
| 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 | PPIC_ECOLI |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–92； UniProt 1–92 |
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 | 1jnt |
| Deposition date deposition_date | 2001-07-25 |
| Structure title title | NMR Structure of the E. coli Peptidyl-Prolyl cis/trans-Isomerase Parvulin 10 |
| Keywords keywords | ALPHA-BETA SANDWICH, CIS PEPTIDE BOND, ISOMERASE; ISOMERASE |
| 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） | 14.25 Å |
| Rg (electron density) | 12.85 Å |
| Total Rg | 14.35 Å |
| Atom count | 1451 |
| Residues | 92 |
| Excluded volume | 12870 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1jnta_ |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.26 — FKBP-like |
| Superfamily Superfamily superfamily | d.26.1 — FKBP-like |
| Family Family family | d.26.1.1 — FKBP immunophilin/proline isomerase |
| Domain ID domain_id | 1jntA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 10 — Roll |
| Topology topology | 50 — Chitinase A; domain 3 |
| Homologous superfamily homologous superfamily | 40 — |