BAR/IMD domain-containing adapter protein 2 (BAIAP2) is a 552-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UQB8.
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The mean pLDDT of this model is 71.7 (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 | 50% |
| 70 to 90 | Confident: backbone generally right | 6% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 39% |
What pLDDT means and how to read it
Adapter protein that links membrane-bound small G proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth, neuronal differentiation and neuronal migration (PubMed:41133935). Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. Participates in actin bundling when associated with EPS8, promoting filopodial protrusions (PubMed:41133935)
Homodimer (PubMed:38149472). Interacts with CDC42 and RAC1 that have been activated by GTP binding. Interacts with ATN1, ADGRB1, EPS8, SHANK1, SHANK2, SHANK3, WASF1 and WASF2. Interacts with ENAH after recruitment of CDC42. Interacts with TIAM1 and DIAPH1 (By similarity). Interacts (via SH3 domain) with E.coli effector protein EspF(U) (via PXXP motifs). Interacts with E.coli intimin receptor Tir
Cytoplasm, Membrane, Cell projection, filopodium, Cell projection, ruffle, Cytoplasm, cytoskeleton
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6ZEG | X-ray | 1.09 Å | A/B=448-464 |
| 6ZEI | X-ray | 1.39 Å | A/B=448-464 |
| 3RNJ | X-ray | 1.5 Å | A=375-436 |
| 4JS0 | X-ray | 1.9 Å | B=260-291 |
| 6BCR | X-ray | 1.99 Å | C/D/G/H=333-346 |
| 2YKT | X-ray | 2.11 Å | A=1-250 |
| 1Y2O | X-ray | 2.2 Å | A/B=1-250 |
| 6BCY | X-ray | 2.3 Å | C/D/G/H=354-366 |
| 6BD1 | X-ray | 2.35 Å | C/D/G/H=360-373 |
| 1WDZ | X-ray | 2.63 Å | A/B=1-228 |
| 6BQT | X-ray | 2.8 Å | C/F/I/L=335-366 |
| 6BD2 | X-ray | 2.9 Å | C=335-372 |
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