Escherichia coli
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein–DNA | Monomer | Protein 1 DNA 1 | DNA (25-MER) × 1 NICKEL (II) ION × 1 water × 2 | Consistent with all polymers |
| UniProt name | Q47673_ECOLI |
| Isoform | — |
| PDB entities | 2 |
| 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 | 1s6m |
| Deposition date deposition_date | 2004-01-26 |
| Structure title title | Conjugative Relaxase Trwc In Complex With Orit DNA. Metal-Bound Structure |
| Keywords keywords | protein-dna complex, bacterial conjugation, relaxase, dna replication, DNA BINDING PROTEIN-DNA COMPLEX; DNA BINDING PROTEIN/DNA |
| 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） | 22.94 Å |
| Rg (electron density) | 21.88 Å |
| Total Rg | 22.56 Å |
| Atom count | 2789 |
| Residues | 309 |
| Excluded volume | 47412 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1s6ma_ |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.89 — Origin of replication-binding domain, RBD-like |
| Superfamily Superfamily superfamily | d.89.1 — Origin of replication-binding domain, RBD-like |
| Family Family family | d.89.1.5 — Relaxase domain |