1vjq
Designed protein based on backbone conformation of procarboxypeptidase-A (1AYE) with sidechains chosen for maximal predicted stability.
1. Protein Identity and Related Structures Protein Identity & Related Structures
No usable UniProt protein identity is available for this entry.
The relationship tables retain this entry's assembly and composition data, but cross-PDB links for the same protein cannot be established reliably without a unified protein identity.
Assembly Composition of the Current Entry
| Assembly | Physical composition | Protein state | 蛋白 / DNA / RNA / 其他Polymer | Data consistency |
|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | 2 / 0 / 0 / 0 | Consistent with protein count |
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.
2. Structure Basics 2. Structure Basics
| Entry ID entry_id | 1vjq |
| Deposition date deposition_date | 2004-03-19 |
| Structure title title | Designed protein based on backbone conformation of procarboxypeptidase-A (1AYE) with sidechains chosen for maximal predicted stability. |
| Keywords keywords | ;STRUCTURAL GENOMICS, ENGINEERED PROTEIN, PSI, Protein Structure Initiative, Structural Genomics of Pathogenic Protozoa Consortium, SGPP, DE NOVO PROTEIN ;; STRUCTURAL GENOMICS, DE NOVO PROTEIN |
| Experimental Method method | X-RAY DIFFRACTION |
3. Official assembly/model SAXS Official SAXS Profiles
This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.
1vjq__assembly_1__model_1
Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)
1vjq__assembly_1__model_1 | I(q)
1vjq__assembly_1__model_1 | P(r) · Pending
| Rg（Guinier） | 17.00 Å |
| Rg (electron density) | 15.62 Å |
| Total Rg | 16.84 Å |
| Atom count | 1162 |
| Residues | 142 |
| Excluded volume | 21073 ų |
| Maximum q | 0.500 Å⁻¹ |
4. Crystallography and Experiment 4. Crystallography & Experiment
5. Entities and Polymers Entities & Polymers (2)
6. Fold Classification (SCOP + CATH) 4 domains
SCOP 2.08 (2 domains)
| Domain ID domain_id | d1vjqa_ |
| Class class | k — Designed proteins |
| Fold Fold fold | k.43 — Carboxypeptidase A prodomain-based design |
| Superfamily Superfamily superfamily | k.43.1 — Carboxypeptidase A prodomain-based design |
| Family Family family | k.43.1.1 — Carboxypeptidase A prodomain-based design |
| Domain ID domain_id | d1vjqb_ |
| Class class | k — Designed proteins |
| Fold Fold fold | k.43 — Carboxypeptidase A prodomain-based design |
| Superfamily Superfamily superfamily | k.43.1 — Carboxypeptidase A prodomain-based design |
| Family Family family | k.43.1.1 — Carboxypeptidase A prodomain-based design |
CATH v4.4 (2 domains)
| Domain ID domain_id | 1vjqA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 70 — Alpha-Beta Plaits |
| Homologous superfamily homologous superfamily | 340 — Metallocarboxypeptidase-like |
| Domain ID domain_id | 1vjqB00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 70 — Alpha-Beta Plaits |
| Homologous superfamily homologous superfamily | 340 — Metallocarboxypeptidase-like |