Crystal structure of the rod domain of alpha-actinin. Determined by X-ray diffraction at 2.8 Å resolution. Released 27 Jun 2001.
Explore 1HCI in 3D Show helices and sheets RCSB PDB PDBe
1HCI contains 34 α-helices and 0 β-strands across 2 chains. 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 | 275-294 | 20 | |
| α-helix | 296-303 | 8 | |
| α-helix | 318-325 | 8 | |
| α-helix | 326-330 | 5 | |
| α-helix | 331-340 | 10 | |
| α-helix | 344-347 | 4 | |
| α-helix | 364-366 | 3 | |
| α-helix | 371-382 | 12 | |
| α-helix | 385-417 | 33 | |
| α-helix | 420-425 | 6 | |
| α-helix | 428-430 | 3 | |
| α-helix | 434-470 | 37 | |
| α-helix | 476-538 | 63 | |
| α-helix | 548-587 | 40 | |
| α-helix | 604-661 | 58 | |
| α-helix | 672-704 | 33 | |
| α-helix | 716-741 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-actinin 2 | A, B | protein | 476 | HOMO SAPIENS | P35609 (AlphaFold model) |
>1HCI_1 ALPHA-ACTININ 2 (chains A, B) GSSAVNQENERLMEEYERLASELLEWIRRTIPWLENRTPEKTMQAMQKKLEDFRDYRRKH KPPKVQEKCQLEINFNTLQTKLRISNRPAFMPSEGKMVSDIAGAWQRLEQAEKGYEEWLL NEIRRLERLEHLAEKFRQKASTHETWAYGKEQILLQKDYESASLTEVRALLRKHEAFESD LAAHQDRVEQIAAIAQELNELDYHDAVNVNDRCQKICDQWDRLGTLTQKRREALERMEKL LETIDQLHLEFAKRAAPFNNWMEGAMEDLQDMFIVHSIEEIQSLITAHEQFKATLPEADG ERQSIMAIQNEVEKVIQSYNIRISSSNPYSTVTMDELRTKWDKVKQLVPIRDQSLQEELA RQHANERLRRQFAAQANAIGPWIQNKMEEIARSSIQITGALEDQMNQLKQYEHNIINYKN NIDKLEGDHQLIQEALVFDNKHTNYTMEHIRVGWELLLTTIARTINEVETQILTRD
Crystal Structure of the Alpha-Actinin Rod Reveals an Extensive Torsional Twist. Ylanne, J., Scheffzek, K., Young, P. et al. Structure (2001) 9:597. DOI 10.1016/S0969-2126(01)00619-0 · 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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