Arabidopsis thaliana
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | 1,2-ETHANEDIOL × 1 water × 1 | Consistent with protein count |
| UniProt name | Q9LZX1_ARATH |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–217； UniProt 1–217 |
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 | 1zxu |
| Deposition date deposition_date | 2005-06-08 |
| Structure title title | X-ray structure of protein from arabidopsis thaliana AT5G01750 |
| Keywords keywords | ;AT5G01750, PFAM PF01167, TULP, STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, PSI, CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS, CESG, UNKNOWN FUNCTION ;; STRUCTURAL GENOMICS, UNKNOWN FUNCTION |
| 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） | 16.22 Å |
| Rg (electron density) | 14.76 Å |
| Total Rg | 15.93 Å |
| Atom count | 1291 |
| Residues | 160 |
| Excluded volume | 23088 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1zxua1 |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.23 — Tubby C-terminal domain-like |
| Superfamily Superfamily superfamily | d.23.1 — Tubby C-terminal domain-like |
| Family Family family | d.23.1.2 — At5g01750-like |
| Domain ID domain_id | 1zxuA00 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 40 — Beta Barrel |
| Topology topology | 160 — Porin |
| Homologous superfamily homologous superfamily | 200 — LURP1-related |