Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) is a 163-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13526.
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The mean pLDDT of this model is 91.6 (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 | 86% |
| 70 to 90 | Confident: backbone generally right | 4% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 6% |
What pLDDT means and how to read it
Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs (PubMed:21497122, PubMed:23623683, PubMed:29686383). By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes (PubMed:21497122, PubMed:22033920, PubMed:23623683). Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK (PubMed:16644721). Can transactivate multiple oncogenes and induce centrosome…
Interacts with STIL (By similarity). Interacts with KIF20B (PubMed:11470801). Interacts with NEK6 (PubMed:16476580). Interacts (via WW domain) with PRKX (PubMed:19367327). Interacts with BTK (PubMed:16644721). Interacts (via PpiC domain) with DAPK1 (PubMed:21497122). Interacts with the phosphorylated form of RAF1 (PubMed:15664191). Interacts (via WW domain) with ATCAY; upon NGF stimulation…
Nucleus, Nucleus speckle, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7AZ2 | X-ray | 1.08 Å | P=61-77 |
| 7AZ1 | X-ray | 1.15 Å | P=61-77 |
| 3I6C | X-ray | 1.3 Å | A/B=45-163 |
| 4TNS | X-ray | 1.33 Å | A/B=43-163 |
| 1PIN | X-ray | 1.35 Å | A=1-163 |
| 3TC5 | X-ray | 1.4 Å | A=1-163 |
| 7AXN | X-ray | 1.4 Å | P=61-77 |
| 7BG3 | X-ray | 1.4 Å | P=61-77 |
| 6VAJ | X-ray | 1.42 Å | A=1-163 |
| 9KFZ | X-ray | 1.43 Å | A=1-163 |
| 2ITK | X-ray | 1.45 Å | A=1-163 |
| 2ZQT | X-ray | 1.46 Å | A=1-163 |
| 2F21 | X-ray | 1.5 Å | A=1-163 |
| 2Q5A | X-ray | 1.5 Å | A=1-163 |
| 5VTJ | X-ray | 1.5 Å | A=6-39 |
| 7AOG | X-ray | 1.5 Å | P=61-77 |
| 9JJS | X-ray | 1.52 Å | A/B=45-163 |
| 9KEQ | X-ray | 1.53 Å | A=1-163 |
| 9KX7 | X-ray | 1.53 Å | A=1-163 |
| 9KXC | X-ray | 1.53 Å | A=1-163 |
Showing 20 of 186 experimental structures (best resolution first).
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