5NC7: ENAH EVH1
ENAH EVH1 in complex with Ac-WPPPPTEDEL-NH2. Determined by X-ray diffraction at 2.7 Å resolution. Released 21 Mar 2018.
- Method
- X-ray diffraction
- Resolution
- 2.7 Å
- Organisms
- Homo sapiens, Listeria monocytogenes
- Chains
- 12
- Atoms
- 3,989
- Mol. weight
- 60.15 kDa
- Released
- 21 Mar 2018
Explore 5NC7 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5NC7 contains 12 α-helices and 32 β-strands across 10 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.
Chain A: 1 helix, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-17 | 14 | 1 |
| β-strand | 22-25 | 4 | 1 |
| 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 | 94-110 | 17 | |
Chain B: 2 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-17 | 14 | 2 |
| β-strand | 22-25 | 4 | 2 |
| α-helix | 26-28 | 3 | |
| β-strand | 33-40 | 8 | 2 |
| β-strand | 45-52 | 8 | 2 |
| β-strand | 58-64 | 7 | 2 |
| β-strand | 71 | 1 | 2 |
| β-strand | 77-81 | 5 | 2 |
| β-strand | 86-91 | 6 | 2 |
| α-helix | 94-110 | 17 | |
Chain C: 2 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-17 | 15 | 3 |
| β-strand | 22-25 | 4 | 3 |
| α-helix | 26-28 | 3 | |
| β-strand | 32-40 | 9 | 3 |
| β-strand | 45-52 | 8 | 3 |
| β-strand | 58-64 | 7 | 3 |
| β-strand | 70-71 | 2 | 3 |
| β-strand | 77-81 | 5 | 3 |
| β-strand | 86-91 | 6 | 3 |
| α-helix | 94-110 | 17 | |
Chain D: 1 helix, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-17 | 15 | 4 |
| β-strand | 22-25 | 4 | 4 |
| β-strand | 33-40 | 8 | 4 |
| β-strand | 45-52 | 8 | 4 |
| β-strand | 58-64 | 7 | 4 |
| β-strand | 70-71 | 2 | 4 |
| β-strand | 77-81 | 5 | 4 |
| β-strand | 86-91 | 6 | 4 |
| α-helix | 94-110 | 17 | |
Chains I, J, K and L: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-6 | 5 | |
Chains X and Z: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-4 | 3 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Protein enabled homolog | A, B, C, D | protein | 113 | Homo sapiens | Q8N8S7 (AlphaFold model) |
| ActA-derived 10-mer Ac-FPPPPTEDEL-NH2 with acetylated (Ac) and amidated (NH2) termini. Phe is… | I, J, K, L, W, X, Y, Z | protein | 12 | Listeria monocytogenes | P33379 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>5NC7_1 Protein enabled homolog (chains A, B, C, D)
GSMSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQV
VINCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVL
Sequence of entity 2 (I, J, K, L, W, X, Y, Z), FASTA
>5NC7_2 ActA-derived 10-mer Ac-FPPPPTEDEL-NH2 with acetylated (Ac) and amidated (NH2) termini. Phe is substitued by Trp to increase affinity for crystallization (chains I, J, K, L, W, X, Y, Z)
XWPPPPTEDELX
Primary citation
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:
- 7A5M 0.78 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-17]-OMe
- 6RD2 1.0 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-1]-TEDEL-NH2
- 5NCG 1.02 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-9]-OH
- 6RCF 1.1 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-15]-OH
- 5NBF 1.15 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-3]-OH
- 5N9C 1.16 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-PP-[ProM-1]-OH
- 5NEG 1.29 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-13]-OEt
- 2HO2 1.33 Å, Structure of human FE65-WW domain in complex with hMena peptide.
- 6RCJ 1.35 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-15]-OMe
- 7AKI 1.36 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-1]-NH2
- 5NCF 1.4 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-4]-OH
- 6XVT 1.4 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-PPPPTEDDL-NH2
Browse structure collections
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