Protein enabled homolog (ENAH) is a 591-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8N8S7.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 70.6 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 41% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 35% |
What pLDDT means and how to read it
Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation (By similarity)
Homotetramer (By similarity). Interacts with APBB1IP, APBB1, PFN1 and ROBO4 (PubMed:12941633, PubMed:15469846, PubMed:17686488). Isoforms, containing the polyproline-rich regions with PPLP motifs, bind the WW domain of APBB1IP (PubMed:15469846). Isoforms, containing the PPSY motif, bind, in vitro, to the WW2 and WW3 domains of NEDD4 and to the WW1 domain of YAP1 (By similarity). Binds the SH3…
Cytoplasm, Cytoplasm, cytoskeleton, Cell projection, lamellipodium, Cell projection, filopodium, Synapse, Cell junction, focal adhesion
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7A5M | X-ray | 0.78 Å | A=1-111 |
| 6RD2 | X-ray | 1.0 Å | A/B=1-111 |
| 5NCG | X-ray | 1.02 Å | A/B=1-111 |
| 6RCF | X-ray | 1.1 Å | A=1-111 |
| 5NBF | X-ray | 1.15 Å | A=1-111 |
| 5N9C | X-ray | 1.16 Å | A/B=1-111 |
| 5NEG | X-ray | 1.29 Å | A/B=1-111 |
| 2HO2 | X-ray | 1.33 Å | B=347-356 |
| 6RCJ | X-ray | 1.35 Å | A=1-111 |
| 7AKI | X-ray | 1.36 Å | A=1-111 |
| 5NCF | X-ray | 1.4 Å | A/B=1-111 |
| 6XVT | X-ray | 1.4 Å | A/B=1-111 |
| 9C66 | X-ray | 1.4 Å | A=1-113 |
| 5NDU | X-ray | 1.42 Å | A/B=1-111 |
| 5ND0 | X-ray | 1.45 Å | A/B=1-111 |
| 5NAJ | X-ray | 1.46 Å | A/B/C/D=1-111 |
| 6XXR | X-ray | 1.48 Å | A/B=1-111 |
| 5N91 | X-ray | 1.49 Å | A/B=1-111 |
| 5NC2 | X-ray | 1.58 Å | A/B=1-111 |
| 5NBX | X-ray | 1.65 Å | A/B=1-111 |
Showing 20 of 27 experimental structures (best resolution first).
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