Escherichia coli
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | water × 1 | Consistent with protein count |
| UniProt name | RNH_ECOLI |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–155； UniProt 1–155 |
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 | 1kva |
| Deposition date deposition_date | 1996-10-04 |
| Structure title title | E. COLI RIBONUCLEASE HI D134A MUTANT |
| Keywords keywords | HYDROLASE, ENDORIBONUCLEASE, MUTANT; ENDORIBONUCLEASE |
| 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） | 16.69 Å |
| Rg (electron density) | 15.59 Å |
| Total Rg | 16.75 Å |
| Atom count | 1235 |
| Residues | 155 |
| Excluded volume | 21795 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1kvaa_ |
| Class class | c — Alpha and beta proteins (a/b) |
| Fold Fold fold | c.55 — Ribonuclease H-like motif |
| Superfamily Superfamily superfamily | c.55.3 — Ribonuclease H-like |
| Family Family family | c.55.3.1 — Ribonuclease H |
| Domain ID domain_id | 1kvaA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 420 — Nucleotidyltransferase; domain 5 |
| Homologous superfamily homologous superfamily | 10 — Ribonuclease H-like superfamily/Ribonuclease H |