5A4B
Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and incorporation in muscle.
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B (A, B) | HUMAN ALPHA-ACTININ-2 | polymer | 248 | 28462.8 | 2 | UniProt (P35609) Pfam (PF00307) | HOMO SAPIENS (HUMAN) | ALPHA-ACTININ SKELETAL MUSCLE ISOFORM 2, F-ACTIN CROSS-LINKING PROTEIN, HUMAN ALPHA-ACTININ-2 |
| 2 | C, D (A, B) | water | water | 18.0 | 201 | Chemie (HOH) |
Sequence modifications
A, B: 19 - 266 (UniProt: P35609)
| PDB | External Database | Details |
|---|---|---|
| Thr 119 | Ala 119 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 56925.5 | |
| All* | Total formula weight | 56925.5 |
