Polyadenylate-binding protein 1 (PABPC1) is a 636-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P11940.
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The mean pLDDT of this model is 77.4 (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 | 49% |
| 70 to 90 | Confident: backbone generally right | 22% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 25% |
What pLDDT means and how to read it
Binds the poly(A) tail of mRNA, including that of its own transcript, and regulates processes of mRNA metabolism such as pre-mRNA splicing and mRNA stability (PubMed:11051545, PubMed:17212783, PubMed:25480299). Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2 (PubMed:11051545, PubMed:20573744). Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (PubMed:32245947). Involved in translationally coupled mRNA turnover (PubMed:11051545). Implicated with other RNA-binding proteins in the…
May form homodimers. Component of a multisubunit autoregulatory ribonucleoprotein complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1 (PubMed:16356927). Directly interacts with IGF2BP1; the interaction is enhanced by SEPIN14P20 peptide RBPR (PubMed:29476152, PubMed:32245947). Part of a complex associated with the FOS mCRD domain and consisting of HNRPD, SYNCRIP, PAIP1 and CSDE1/UNR…
Cytoplasm, Cytoplasm, Stress granule, Nucleus, Cell projection, lamellipodium
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3KUJ | X-ray | 1.4 Å | A=544-626 |
| 3KUS | X-ray | 1.4 Å | A/B=544-626 |
| 2X04 | X-ray | 1.49 Å | A/B=545-619 |
| 3KTP | X-ray | 1.5 Å | A=544-626 |
| 3KUT | X-ray | 1.5 Å | A/B=544-626 |
| 3KTR | X-ray | 1.7 Å | A=544-626 |
| 3PTH | X-ray | 1.7 Å | A=543-621 |
| 3PKN | X-ray | 1.8 Å | A=544-626 |
| 4F25 | X-ray | 1.9 Å | A=99-199 |
| 5DX1 | X-ray | 1.93 Å | F/G/H/I=449-466 |
| 7BN3 | X-ray | 1.93 Å | A/B/C=544-626 |
| 5DX8 | X-ray | 1.94 Å | E/F/G/H=449-466 |
| 4F02 | X-ray | 2.0 Å | A/D=1-190 |
| 4F26 | X-ray | 2.0 Å | A=99-199 |
| 5LGR | X-ray | 2.0 Å | E/F/G/H=447-458 |
| 5LGP | X-ray | 2.04 Å | E/F/G/H=447-459 |
| 5DXA | X-ray | 2.07 Å | F/G/I=449-466 |
| 5LGS | X-ray | 2.1 Å | E/F/G/H=456-464 |
| 5LGQ | X-ray | 2.11 Å | E/F/G/H=456-466 |
| 3KUI | X-ray | 2.3 Å | A=544-626 |
Showing 20 of 29 experimental structures (best resolution first).
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