Serine/threonine-protein phosphatase 5 (PPP5C) is a 499-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P53041.
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The mean pLDDT of this model is 92.8 (very high 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 | 84% |
| 70 to 90 | Confident: backbone generally right | 10% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT (PubMed:14734805, PubMed:14764652, PubMed:14871926, PubMed:15383005, PubMed:15546861, PubMed:16260606, PubMed:16790549, PubMed:16892053, PubMed:19176521, PubMed:19948726, PubMed:21144835, PubMed:22399290, PubMed:22781750, PubMed:23102700, PubMed:30699359, PubMed:9000529). Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian…
Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (PubMed:29127155). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23…
Nucleus, Cytoplasm, Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4ZX2 | X-ray | 1.23 Å | A=169-499 |
| 3H63 | X-ray | 1.3 Å | A/C=176-490 |
| 3H62 | X-ray | 1.4 Å | B/C=176-490 |
| 3H61 | X-ray | 1.45 Å | A/D=176-490 |
| 3H68 | X-ray | 1.5 Å | A/D=176-490 |
| 1S95 | X-ray | 1.6 Å | A/B=169-499 |
| 3H67 | X-ray | 1.65 Å | A/D=176-490 |
| 5WG8 | X-ray | 1.65 Å | A=169-499 |
| 3H64 | X-ray | 1.9 Å | A/D=176-490 |
| 5UI1 | X-ray | 1.96 Å | A/B/C/D=169-499 |
| 3H60 | X-ray | 2.0 Å | A/B=176-490 |
| 4ZVZ | X-ray | 2.0 Å | A/B/C/D=169-499 |
| 3H69 | X-ray | 2.1 Å | A/D=176-490 |
| 5HPE | X-ray | 2.27 Å | A=175-499 |
| 1A17 | X-ray | 2.45 Å | A=16-181 |
| 3H66 | X-ray | 2.59 Å | A/B=176-490 |
| 1WAO | X-ray | 2.9 Å | 1/2/3/4=23-499 |
| 8GAE | EM | 3.3 Å | E=1-499 |
| 8GFT | EM | 3.8 Å | E=1-499 |
| 7ZR5 | EM | 3.9 Å | P=17-499 |
Showing 20 of 22 experimental structures (best resolution first).
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