EVH1 domain from murine enabled in complex with acta peptide. Determined by X-ray diffraction at 1.8 Å resolution. Released 21 May 1999.
Explore 1EVH in 3D Show helices and sheets RCSB PDB PDBe
1EVH contains 3 α-helices and 8 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 |
|---|---|---|---|
| β-strand | 3-17 | 15 | 1 |
| β-strand | 22-25 | 4 | 1 |
| α-helix | 26-28 | 3 | |
| β-strand | 33-40 | 8 | 1 |
| β-strand | 45-52 | 8 | 1 |
| β-strand | 58-64 | 7 | 1 |
| β-strand | 71 | 1 | 1 |
| β-strand | 77-81 | 5 | 1 |
| β-strand | 86-91 | 6 | 1 |
| α-helix | 94-111 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1002-1004 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (mena EVH1 domain) | A | protein | 112 | Mus musculus | Q03173 (AlphaFold model) |
| Peptide ACTA | B | protein | 7 |
>1EVH_1 PROTEIN (MENA EVH1 DOMAIN) (chains A) MSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVI NCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVLN
>1EVH_2 Peptide ACTA (chains B) XFPPPPT
Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly. Prehoda, K.E., Lee, D.J., Lim, W.A. Cell (1999) 97:471-480. DOI 10.1016/S0092-8674(00)80757-6 · PubMed
Other PDB entries of the same protein (UniProt Q03173 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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