Heat shock protein HSP 90-alpha (HSP90AA1) is a 732-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P07900.
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The mean pLDDT of this model is 85.2 (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 | 60% |
| 70 to 90 | Confident: backbone generally right | 25% |
| 50 to 70 | Low: treat with caution | 6% |
| 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 that is linked to its ATPase activity which is essential for its chaperone 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:11274138, PubMed:12526792, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). Engages with a range of client protein classes via…
Homodimer (PubMed:18400751, PubMed:29127155, PubMed:7588731, PubMed:8289821). Identified in NR3C1/GCR steroid receptor-chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C or STIP1 (PubMed:15383005, PubMed:9195923). Forms a complex containing HSP90AA1, TSC1 and TSC2; TSC1 is required to recruit TCS2 to the…
Nucleus, Cytoplasm, Melanosome, Cell membrane, Mitochondrion
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5J80 | X-ray | 1.17 Å | A=9-233 |
| 6TN5 | X-ray | 1.17 Å | AAA=9-236 |
| 3T0H | X-ray | 1.2 Å | A=9-236 |
| 5J2X | X-ray | 1.22 Å | A=17-224 |
| 3T10 | X-ray | 1.24 Å | A=9-236 |
| 6TN4 | X-ray | 1.27 Å | AAA=9-236 |
| 3WHA | X-ray | 1.3 Å | A/B=9-236 |
| 5XRD | X-ray | 1.3 Å | A=9-236 |
| 2YK9 | X-ray | 1.32 Å | A=18-223 |
| 5LRL | X-ray | 1.33 Å | A=18-223 |
| 6GR5 | X-ray | 1.34 Å | A=1-236 |
| 3B28 | X-ray | 1.35 Å | A/B=9-236 |
| 5J64 | X-ray | 1.38 Å | A=9-236 |
| 7HBS | X-ray | 1.38 Å | A=9-236 |
| 7HBT | X-ray | 1.38 Å | A=9-236 |
| 3VHA | X-ray | 1.39 Å | A=9-236 |
| 1UYL | X-ray | 1.4 Å | A=1-236 |
| 2YI7 | X-ray | 1.4 Å | A=1-229 |
| 3VHC | X-ray | 1.41 Å | A=9-236 |
| 7H9L | X-ray | 1.42 Å | A=9-236 |
Showing 20 of 446 experimental structures (best resolution first).
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