Heat shock protein HSP 90-beta (HSP90AB1) is a 724-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P08238.
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The mean pLDDT of this model is 84.3 (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 | 57% |
| 70 to 90 | Confident: backbone generally right | 27% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 9% |
What pLDDT means and how to read it
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with…
Monomer (PubMed:24880080). Homodimer (PubMed:18400751, PubMed:7588731). Forms a complex with CDK6 and CDC37 (PubMed:25486457, PubMed:9482106). Interacts with UNC45A; binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer (PubMed:16478993). Interacts with CHORDC1 (By similarity). Interacts with DNAJC7 (PubMed:18620420). Interacts with FKBP4 (PubMed:15159550). May interact with NWD1…
Cytoplasm, Melanosome, Nucleus, Secreted, Cell membrane, Dynein axonemal particle, Cell surface
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9D9I | X-ray | 1.5 Å | A=1-223 |
| 6N8Y | X-ray | 1.55 Å | A=1-221 |
| 5UCJ | X-ray | 1.69 Å | A/B/C/D=1-218 |
| 7ULJ | X-ray | 1.82 Å | A/B/C/D=1-218 |
| 9D9H | X-ray | 1.96 Å | A=1-223 |
| 5UC4 | X-ray | 2.05 Å | A/B/C/D=1-218 |
| 3FWV | X-ray | 2.2 Å | C/D=720-724 |
| 3NMQ | X-ray | 2.2 Å | A=1-223 |
| 3PRY | X-ray | 2.28 Å | A/B/C=284-543 |
| 1UYM | X-ray | 2.45 Å | A=2-221 |
| 3UQ3 | X-ray | 2.6 Å | B/C=720-724 |
| 9W5I | EM | 2.63 Å | A/B=1-724 |
| 5UCH | X-ray | 2.65 Å | A/B/C/D=1-218 |
| 5UCI | X-ray | 2.7 Å | A/B/C/D=1-218 |
| 8QMO | EM | 2.76 Å | A/B=2-724 |
| 7ZUB | EM | 2.85 Å | A/B=2-724 |
| 1QZ2 | X-ray | 3.0 Å | G/H=720-724 |
| 6N8W | X-ray | 3.09 Å | A/B/C/D=1-231 |
| 8EOB | EM | 3.1 Å | A/B=2-724 |
| 7Z38 | EM | 3.16 Å | A/B=3-724 |
Showing 20 of 32 experimental structures (best resolution first).
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