ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-9]-OH. Determined by X-ray diffraction at 1.02 Å resolution. Released 21 Mar 2018.
Explore 5NCG in 3D Show helices and sheets RCSB PDB PDBe
5NCG contains 6 α-helices and 16 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 | 0-2 | 3 | |
| β-strand | 3-17 | 15 | 1 |
| β-strand | 22-25 | 4 | 1 |
| α-helix | 26-28 | 3 | |
| β-strand | 32-40 | 9 | 1 |
| β-strand | 45-52 | 8 | 1 |
| β-strand | 58-64 | 7 | 1 |
| β-strand | 70-72 | 3 | 1 |
| β-strand | 77-81 | 5 | 1 |
| β-strand | 86-91 | 6 | 1 |
| α-helix | 94-110 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 0-2 | 3 | |
| β-strand | 3-17 | 15 | 2 |
| β-strand | 22-25 | 4 | 2 |
| α-helix | 26-28 | 3 | |
| β-strand | 32-40 | 9 | 2 |
| β-strand | 45-52 | 8 | 2 |
| β-strand | 58-63 | 6 | 2 |
| β-strand | 70-72 | 3 | 2 |
| β-strand | 77-81 | 5 | 2 |
| β-strand | 86-91 | 6 | 2 |
| α-helix | 94-108 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein enabled homolog | A, B | protein | 113 | Homo sapiens | Q8N8S7 (AlphaFold model) |
>5NCG_1 Protein enabled homolog (chains A, B) GSMSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQV VINCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVL
| ID | Name | Formula | Copies |
|---|---|---|---|
| 8TB | (3~{S},7~{R},10~{R},11~{R},13~{S})-4-[(3~{S},6~{R},8~{a}~{S})-1'-[(2~{S})-2-ace… | C36 H42 Cl N5 O7 | 5 |
Water and common crystallization additives (NO3) are not listed.
Designed nanomolar small-molecule inhibitors of Ena/VASP EVH1 interaction impair invasion and extravasation of breast cancer cells. Barone, M., Muller, M., Chiha, S. et al. Proc Natl Acad Sci U S A (2020) 117:29684-29690. DOI 10.1073/pnas.2007213117 · PubMed
Other PDB entries of the same protein (UniProt Q8N8S7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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