Bifidobacterium longum NCC2705
| 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 | Q8G4D5_BIFLO |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 4–450； UniProt 2–448 |
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 | 2p9b |
| Deposition date deposition_date | 2007-03-24 |
| Structure title title | Crystal structure of putative prolidase from Bifidobacterium longum |
| Keywords keywords | ;Protein Structure Initiative II, PSI-2, 9350a, Amidohydrolase, Prolidase, Structural Genomics, New York SGX Research Center for Structural Genomics, NYSGXRC, 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） | 21.74 Å |
| Rg (electron density) | 20.79 Å |
| Total Rg | 21.59 Å |
| Atom count | 2988 |
| Residues | 397 |
| Excluded volume | 53365 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d2p9ba1 |
| Class class | b — All beta proteins |
| Fold Fold fold | b.92 — Composite domain of metallo-dependent hydrolases |
| Superfamily Superfamily superfamily | b.92.1 — Composite domain of metallo-dependent hydrolases |
| Family Family family | b.92.1.10 — Imidazolonepropionase-like |
| Domain ID domain_id | d2p9ba2 |
| Class class | c — Alpha and beta proteins (a/b) |
| Fold Fold fold | c.1 — TIM beta/alpha-barrel |
| Superfamily Superfamily superfamily | c.1.9 — Metallo-dependent hydrolases |
| Family Family family | c.1.9.17 — Imidazolonepropionase-like |
| Domain ID domain_id | 2p9bA01 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 30 — Roll |
| Topology topology | 40 — Urease, subunit C; domain 1 |
| Homologous superfamily homologous superfamily | 10 — Urease, subunit C, domain 1 |
| Domain ID domain_id | 2p9bA02 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 110 — Translation Initiation Factor IF3 |
| Homologous superfamily homologous superfamily | 90 — Amidohydrolase |
| Domain ID domain_id | 2p9bA03 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| Topology topology | 50 — Rossmann fold |
| Homologous superfamily homologous superfamily | 10910 — Amidohydrolase |
| Domain ID domain_id | 2p9bA04 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 20 — Up-down Bundle |
| Topology topology | 58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1 |
| Homologous superfamily homologous superfamily | 520 — Amidohydrolase |