Mus musculus
| 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 | FAK1_MOUSE |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–126； UniProt 921–1046 |
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 | 1k40 |
| Deposition date deposition_date | 2001-10-04 |
| Structure title title | crystal structure of the FAT domain of focal adhesion kinase |
| Keywords keywords | HELIX BUNDLE, TRANSFERASE; TRANSFERASE |
| 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） | 17.13 Å |
| Rg (electron density) | 16.54 Å |
| Total Rg | 17.44 Å |
| Atom count | 976 |
| Residues | 126 |
| Excluded volume | 17764 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1k40a_ |
| Class class | a — All alpha proteins |
| Fold Fold fold | a.24 — Four-helical up-and-down bundle |
| Superfamily Superfamily superfamily | a.24.14 — FAT domain of focal adhesion kinase |
| Family Family family | a.24.14.1 — FAT domain of focal adhesion kinase |
| Domain ID domain_id | 1k40A00 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 20 — Up-down Bundle |
| Topology topology | 120 — Four Helix Bundle (Hemerythrin (Met), subunit A) |
| Homologous superfamily homologous superfamily | 330 — Nucleotidyltransferases domain 2 |