Mus musculus
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein heterocomplex | Heteromer | Protein 2 | CD44 antigen × 1 （P15379） water × 2 | Consistent with protein count |
| UniProt name | RADI_MOUSE |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 3–312； UniProt 1–310 |
OrganismNot specified
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein heterocomplex | Heteromer | Protein 2 | Radixin × 1 （P26043） water × 2 | Consistent with protein count |
| UniProt name | CD44_MOUSE |
| Isoform | — |
| PDB entities | 2 |
| Chains and sequence ranges | Author chain B； PDBConstruct 1–20； UniProt 708–727 |
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 | 2zpy |
| Deposition date deposition_date | 2008-07-31 |
| Structure title title | Crystal structure of the mouse radxin FERM domain complexed with the mouse CD44 cytoplasmic peptide |
| Keywords keywords | ;FERM domain, CD44, Actin capping, Actin-binding, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Phosphoprotein, Structural protein, Alternative splicing, Cell adhesion, Glycoprotein, Proteoglycan, Pyrrolidone carboxylic acid, Receptor, Sulfation, Transmembrane ;; CELL ADHESION |
| 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） | 22.72 Å |
| Rg (electron density) | 21.73 Å |
| Total Rg | 22.72 Å |
| Atom count | 2543 |
| Residues | 304 |
| Excluded volume | 45737 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d2zpya1 |
| Class class | a — All alpha proteins |
| Fold Fold fold | a.11 — Acyl-CoA binding protein-like |
| Superfamily Superfamily superfamily | a.11.2 — Second domain of FERM |
| Family Family family | a.11.2.1 — Second domain of FERM |
| Domain ID domain_id | d2zpya2 |
| Class class | b — All beta proteins |
| Fold Fold fold | b.55 — PH domain-like barrel |
| Superfamily Superfamily superfamily | b.55.1 — PH domain-like |
| Family Family family | b.55.1.5 — Third domain of FERM |
| Domain ID domain_id | d2zpya3 |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.15 — beta-Grasp (ubiquitin-like) |
| Superfamily Superfamily superfamily | d.15.1 — Ubiquitin-like |
| Family Family family | d.15.1.4 — First domain of FERM |
| Domain ID domain_id | 2zpyA01 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 10 — Roll |
| Topology topology | 20 — Ubiquitin-like (UB roll) |
| Homologous superfamily homologous superfamily | 90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 |
| Domain ID domain_id | 2zpyA02 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 20 — Up-down Bundle |
| Topology topology | 80 — Acyl-CoA Binding Protein |
| Homologous superfamily homologous superfamily | 10 — |
| Domain ID domain_id | 2zpyA03 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 30 — Roll |
| Topology topology | 29 — PH-domain like |
| Homologous superfamily homologous superfamily | 30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) |