Amyloid beta precursor protein binding family B member 1 (APBB1) is a 710-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O00213.
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The mean pLDDT of this model is 60.1 (low 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 | 29% |
| 70 to 90 | Confident: backbone generally right | 11% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 56% |
What pLDDT means and how to read it
Transcription coregulator that can have both coactivator and corepressor functions (PubMed:15031292, PubMed:18468999, PubMed:18922798, PubMed:25342469, PubMed:33938178). Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain (PubMed:15031292, PubMed:18468999, PubMed:18922798, PubMed:25342469). Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis (PubMed:15031292, PubMed:18468999, PubMed:18922798, PubMed:25342469). May act by specifically recognizing and binding histone H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks (DSBs),…
Component of a complex, at least composed of APBB1, RASD1/DEXRAS1 and APP (PubMed:18468999, PubMed:18833287, PubMed:18922798). Interacts (via PID domain 2) with APP (with the intracellular domain of the amyloid-beta precursor protein) (PubMed:18468999, PubMed:18833287). Interacts (via PID domain 2) with RASD1/DEXRAS1; impairs the transcription activation activity (PubMed:18922798). Interacts…
Cell membrane, Cytoplasm, Nucleus, Cell projection, growth cone, Nucleus speckle
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2HO2 | X-ray | 1.33 Å | A=253-289 |
| 2OEI | X-ray | 1.35 Å | A=253-289 |
| 3DXE | X-ray | 2.0 Å | A/C=534-667 |
| 3DXC | X-ray | 2.1 Å | A/C=534-667 |
| 3D8D | X-ray | 2.2 Å | A/B=366-505 |
| 3DXD | X-ray | 2.2 Å | A/C=534-667 |
| 2IDH | X-ray | 2.28 Å | A/B/C/D/E/F/G/H=253-289 |
| 5NQH | X-ray | 2.6 Å | A/B/C/D=534-667 |
| 3D8F | X-ray | 2.7 Å | A/B/C/D=366-505 |
| 3D8E | X-ray | 2.8 Å | A/B/C/D=366-505 |
| 2E45 | NMR | A=240-290 |
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