Lysosomal acid glucosylceramidase (GBA1) is a 536-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P04062.
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The mean pLDDT of this model is 93.3 (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 | 88% |
| 70 to 90 | Confident: backbone generally right | 3% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 6% |
What pLDDT means and how to read it
Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramides/GlcCers (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) into free ceramides (such as N-acylsphing-4-enine) and glucose (PubMed:15916907, PubMed:24211208, PubMed:32144204, PubMed:39395789, PubMed:9201993). Plays a central role in the degradation of complex lipids and the turnover of cellular membranes (PubMed:27378698). Through the production of ceramides, participates in the PKC-activated salvage pathway of ceramide formation (PubMed:19279011). Catalyzes the glucosylation of cholesterol, through a transglucosylation reaction where glucose is transferred from GlcCer to…
Interacts with saposin-C (PubMed:10781797). Interacts with SCARB2 (PubMed:18022370). Interacts with TCP1 (PubMed:21098288). May interact with SNCA; this interaction may inhibit the glucosylceramidase activity (PubMed:23266198). Interacts with GRN; this interaction prevents aggregation of GBA1-SCARB2 complex via interaction with HSPA1A upon stress (PubMed:27789271)
Lysosome membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6TN1 | X-ray | 0.98 Å | AAA=40-536 |
| 9FB2 | X-ray | 1.14 Å | A=1-536 |
| 9FA3 | X-ray | 1.36 Å | A=1-536 |
| 9FAL | X-ray | 1.39 Å | A=1-536 |
| 9FAY | X-ray | 1.4 Å | A=1-536 |
| 6TJQ | X-ray | 1.41 Å | BBB=40-536 |
| 9FDI | X-ray | 1.41 Å | A=1-536 |
| 8AWR | X-ray | 1.49 Å | AAA=40-536 |
| 9FA6 | X-ray | 1.49 Å | A=1-536 |
| 6TJK | X-ray | 1.56 Å | AAA/BBB=40-536 |
| 8AWK | X-ray | 1.58 Å | AAA=40-536 |
| 6TJJ | X-ray | 1.59 Å | AAA/BBB=40-536 |
| 8AX3 | X-ray | 1.59 Å | A/B=40-536 |
| 6Q6N | X-ray | 1.63 Å | A/B=40-536 |
| 9FAZ | X-ray | 1.63 Å | A=1-536 |
| 6YTP | X-ray | 1.7 Å | AAA/BBB=40-536 |
| 6YTR | X-ray | 1.7 Å | AAA/BBB=40-536 |
| 6Z39 | X-ray | 1.7 Å | AAA/BBB=40-536 |
| 9ENA | X-ray | 1.7 Å | A=40-536 |
| 8P3E | X-ray | 1.75 Å | A/B=40-536 |
Showing 20 of 58 experimental structures (best resolution first).
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