Peptidyl-prolyl cis-trans isomerase A (PPIA) is a 165-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62937.
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The mean pLDDT of this model is 98.1 (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 | 99% |
| 70 to 90 | Confident: backbone generally right | 1% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:2001362, PubMed:20676357, PubMed:21245143, PubMed:21593166, PubMed:25678563). Exerts a strong chemotactic effect on leukocytes partly through activation of one of its membrane receptors BSG/CD147, initiating a signaling cascade that culminates in MAPK/ERK activation (PubMed:11943775, PubMed:21245143). Activates endothelial cells (ECs) in a pro-inflammatory manner by stimulating activation of NF-kappa-B and ERK, JNK and p38 MAP-kinases and by inducing expression of adhesion molecules including SELE and VCAM1 (PubMed:15130913). Induces apoptosis in ECs by promoting the FOXO1-dependent expression of…
Interacts with protein phosphatase PPP3CA/calcineurin A (PubMed:12218175, PubMed:12357034). Interacts with PRPF19 isoform 2 (via N-terminus) (By similarity). Interacts with isoform 2 of BSG/CD147 (PubMed:11353871, PubMed:11943775, PubMed:15688292, PubMed:21245143). Interacts with FOXO1; the interaction promotes FOXO1 dephosphorylation, nuclear accumulation and transcriptional activity…
Cytoplasm, Secreted, Nucleus, Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9E3S | X-ray | 1.08 Å | C/D=1-165 |
| 9BG4 | X-ray | 1.14 Å | C/D=1-165 |
| 4N1M | X-ray | 1.15 Å | A=1-165 |
| 5F66 | X-ray | 1.15 Å | A=1-165 |
| 9GHY | X-ray | 1.15 Å | A=1-165 |
| 6GJL | X-ray | 1.16 Å | A=1-165 |
| 6GS6 | X-ray | 1.16 Å | A=1-165 |
| 2X25 | X-ray | 1.2 Å | B=2-165 |
| 4YUO | X-ray | 1.2 Å | A=1-165 |
| 7UXM | X-ray | 1.2 Å | A/B/C=1-165 |
| 8TBG | X-ray | 1.2 Å | C/D=1-165 |
| 9BFV | X-ray | 1.2 Å | C/D=1-165 |
| 9BFW | X-ray | 1.2 Å | D=1-165 |
| 9BG8 | X-ray | 1.2 Å | C/D=1-165 |
| 3K0M | X-ray | 1.25 Å | A=1-165 |
| 5LUD | X-ray | 1.25 Å | A=1-165 |
| 8TBK | X-ray | 1.26 Å | C/D=1-165 |
| 9BFY | X-ray | 1.26 Å | C/D=1-165 |
| 9CT8 | X-ray | 1.28 Å | C/D=1-165 |
| 6GJY | X-ray | 1.29 Å | A=1-165 |
Showing 20 of 201 experimental structures (best resolution first).
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