Peptidyl-prolyl cis-trans isomerase FKBP1A (FKBP1A) is a 108-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62942.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 96.3 (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 | 98% |
| 70 to 90 | Confident: backbone generally right | 2% |
| 50 to 70 | Low: treat with caution | 0% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides
Interacts with TGFBR1; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation (PubMed:9233797). Interacts with ACVR1B and SMAD7 (PubMed:16720724). Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1) (By similarity). Interacts directly with RYR2 and RYR3 (PubMed:10358090, PubMed:22100703). Interacts with GLMN; rapamycin…
Cytoplasm, cytosol, Sarcoplasmic reticulum membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2PPN | X-ray | 0.92 Å | A=2-108 |
| 2PPP | X-ray | 0.94 Å | A=2-108 |
| 6YF3 | X-ray | 1.0 Å | A=2-108 |
| 6YF2 | X-ray | 1.03 Å | A=2-108 |
| 8X6P | X-ray | 1.05 Å | A/B=1-108 |
| 6YF1 | X-ray | 1.12 Å | A=2-108 |
| 8CHM | X-ray | 1.12 Å | A=2-108 |
| 4N19 | X-ray | 1.2 Å | A=2-108 |
| 8PDF | X-ray | 1.2 Å | A=2-108 |
| 9LYG | X-ray | 1.26 Å | A=1-108 |
| 2PPO | X-ray | 1.29 Å | A=2-108 |
| 7U8D | X-ray | 1.39 Å | A/B=2-108 |
| 9DTW | X-ray | 1.39 Å | B=1-108 |
| 8CHL | X-ray | 1.4 Å | A/B=2-108 |
| 6I1S | X-ray | 1.52 Å | B=1-108 |
| 6YF0 | X-ray | 1.55 Å | A=2-108 |
| 8CHK | X-ray | 1.55 Å | A/B/C=2-108 |
| 1BKF | X-ray | 1.6 Å | A=2-108 |
| 6VCU | X-ray | 1.69 Å | A/B/C/D=1-108 |
| 1FKB | X-ray | 1.7 Å | A=2-108 |
Showing 20 of 108 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.