Crystal structure of two central spectrin-like repeats from alpha-actinin. Determined by X-ray diffraction at 2.5 Å resolution. Released 20 Aug 1999.
Explore 1QUU in 3D Show helices and sheets RCSB PDB PDBe
1QUU contains 7 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-29 | 24 | |
| α-helix | 33-38 | 6 | |
| α-helix | 47-83 | 37 | |
| α-helix | 89-149 | 61 | |
| α-helix | 164-175 | 12 | |
| α-helix | 177-201 | 25 | |
| α-helix | 217-245 | 29 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Human skeletal muscle alpha-actinin 2 | A | protein | 250 | Homo sapiens | P35609 (AlphaFold model) |
>1QUU_1 HUMAN SKELETAL MUSCLE ALPHA-ACTININ 2 (chains A) GSSNEIRRLERLEHLAEKFRQKASTHETWAYGKEQILLQKDYESASLTEVRALLRKHEAF ESDLAAHQDRVEQIAAIAQELNELDYHDAVNVNDRCQKICDQWDRLGTLTQKRREALERM EKLLETIDQLHLEFAKRAAPFNNWMEGAMEDLQDMFIVHSIEEIQSLITAHEQFKATLPE ADGERQSIMAIQNEVEKVIQSYNIRISSSNPYSTVTMDELRTKWDKVKQLVPIRDQSLQE ELARQHANER
Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments. Djinovic-Carugo, K., Young, P., Gautel, M. et al. Cell (1999) 98:537-546. DOI 10.1016/S0092-8674(00)81981-9 · PubMed
Other PDB entries of the same protein (UniProt P35609 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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