BAG family molecular chaperone regulator 1 (BAG1) is a 345-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q99933.
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The mean pLDDT of this model is 62.7 (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 | 6% |
| 70 to 90 | Confident: backbone generally right | 35% |
| 50 to 70 | Low: treat with caution | 26% |
| Below 50 | Very low: often disordered regions | 34% |
What pLDDT means and how to read it
Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70 (PubMed:24318877, PubMed:27474739, PubMed:9873016). Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity (PubMed:12724406). Markedly increases the anti-cell death function of BCL2 induced by various stimuli (PubMed:9305631). Involved in the…
Homodimer. Forms a heteromeric complex with HSP70/HSC70 (PubMed:9305631). Binds to the ATPase domain of HSP/HSC70 chaperones. Isoform 1, isoform 3 and isoform 4 but not isoform 2 interact with HSPA8/HSC70 (PubMed:24318877, PubMed:27474739, PubMed:9305631, PubMed:9679980). Interacts with NR3C1 (PubMed:10477749). Interacts with the N-terminal region of MAPRE2 (PubMed:15986447). Interacts with…
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5AQM | X-ray | 1.63 Å | B/D=222-334 |
| 5AQL | X-ray | 1.69 Å | B/D=222-334 |
| 5AQV | X-ray | 1.75 Å | B=222-334 |
| 5AQF | X-ray | 1.88 Å | B/D=222-334 |
| 1HX1 | X-ray | 1.9 Å | B=222-334 |
| 3LDQ | X-ray | 1.9 Å | B=222-334 |
| 5AQT | X-ray | 1.9 Å | B=222-334 |
| 5AQR | X-ray | 1.91 Å | B/D/F=222-334 |
| 5AQU | X-ray | 1.92 Å | B=222-334 |
| 5AQJ | X-ray | 1.96 Å | B/D/F=222-334 |
| 5AQI | X-ray | 1.98 Å | B/D=222-334 |
| 3FZH | X-ray | 2.0 Å | B=222-334 |
| 5AQH | X-ray | 2.0 Å | B=222-334 |
| 5AQS | X-ray | 2.0 Å | B/D=222-334 |
| 5AQP | X-ray | 2.08 Å | B/D/F=222-334 |
| 5AQK | X-ray | 2.09 Å | B=222-334 |
| 3FZK | X-ray | 2.1 Å | B=222-334 |
| 3M3Z | X-ray | 2.1 Å | B=222-334 |
| 5AQO | X-ray | 2.12 Å | B/D/F=222-334 |
| 3FZF | X-ray | 2.2 Å | B=222-334 |
Showing 20 of 29 experimental structures (best resolution first).
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