Platelet-activating factor acetylhydrolase IB subunit beta (PAFAH1B1) is a 410-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P43034.
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The mean pLDDT of this model is 90.3 (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 | 67% |
| 70 to 90 | Confident: backbone generally right | 26% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition-dependent manner (By similarity). Required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May…
Component of the cytosolic PAF-AH (I) heterotetrameric enzyme, which is composed of PAFAH1B1 (beta), PAFAH1B2 (alpha2) and PAFAH1B3 (alpha1) subunits. The catalytic activity of the enzyme resides in the alpha1 (PAFAH1B3) and alpha2 (PAFAH1B2) subunits, whereas the beta subunit (PAFAH1B1) has regulatory activity. Trimer formation is not essential for the catalytic activity. Interacts with the…
Cytoplasm, cytoskeleton, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Cytoplasm, cytoskeleton, spindle, Nucleus membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7MT1 | X-ray | 1.3 Å | A=86-410 |
| 9E0Z | EM | 2.86 Å | C/D=1-410 |
| 9E11 | EM | 2.86 Å | C/D=1-410 |
| 9DZY | EM | 3.1 Å | C/E=2-410 |
| 9E0T | EM | 3.1 Å | B/C=2-410 |
| 8FDT | EM | 3.2 Å | B/C=2-410 |
| 9E0W | EM | 3.2 Å | C=2-410 |
| 8FDU | EM | 3.3 Å | B/C=2-410 |
| 9E22 | EM | 3.3 Å | E=2-410 |
| 8PQY | EM | 3.8 Å | B/C=1-410 |
| 9YNC | EM | 3.93 Å | C/D/E/F=1-410 |
| 8DYV | EM | 3.97 Å | B=2-410 |
| 8DYU | EM | 4.0 Å | B/C=2-410 |
| 8PQW | EM | 4.2 Å | B/C/D/E=1-410 |
| 9YND | EM | 4.26 Å | B/C/D/E=1-410 |
| 9E13 | EM | 4.5 Å | O/P=1-410 |
| 9E14 | EM | 5.0 Å | O/P=1-410 |
| 8PQZ | EM | 5.5 Å | B/C/D/E/K/L=1-410 |
| 9YNH | EM | 5.5 Å | O/P=1-410 |
| 9YNE | EM | 8.46 Å | B/C=1-410 |
Showing 20 of 21 experimental structures (best resolution first).
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