Paenibacillus polymyxa
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | ZINC ION × 1 water × 1 | Consistent with protein count |
| UniProt name | Q9LCR3_PAEPO |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 2–179； UniProt 322–499 |
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 | 1jwq |
| Deposition date deposition_date | 2001-09-05 |
| Structure title title | Structure of the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus |
| Keywords keywords | open alpha-beta-alpha, 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） | 16.04 Å |
| Rg (electron density) | 14.88 Å |
| Total Rg | 16.00 Å |
| Atom count | 1364 |
| Residues | 179 |
| Excluded volume | 24211 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1jwqa_ |
| Class class | c — Alpha and beta proteins (a/b) |
| Fold Fold fold | c.56 — Phosphorylase/hydrolase-like |
| Superfamily Superfamily superfamily | c.56.5 — Zn-dependent exopeptidases |
| Family Family family | c.56.5.6 — N-acetylmuramoyl-L-alanine amidase-like |
| Domain ID domain_id | 1jwqA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| Topology topology | 630 — Aminopeptidase |
| Homologous superfamily homologous superfamily | 40 — Zn-dependent exopeptidases |