Fructose-bisphosphate aldolase A (ALDOA) is a 364-residue protein from Oryctolagus cuniculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P00883.
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The mean pLDDT of this model is 96.6 (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 | 94% |
| 70 to 90 | Confident: backbone generally right | 4% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Catalyzes the reversible conversion of beta-D-fructose 1,6-bisphosphate (FBP) into two triose phosphate and plays a key role in glycolysis and gluconeogenesis (PubMed:17329259, PubMed:20129922). In addition, also functions as a scaffolding protein (PubMed:17329259). In response to glucose deprivation, FBP dissociates from aldolase and acts as an adapter that promotes AMP-activated protein kinase (AMPK) activity: mechanistically, associates with transient receptor potential channels TrpV (TRPV1-TRPV4), promoting inhibition of the V-ATPase complex on lysosomes and AMPK activation via the AXIN1-STK11/LKB1 axis (By similarity)
Homotetramer (PubMed:10504235, PubMed:18453690, PubMed:20129922, PubMed:2204832). Interacts with SNX9 and WAS. Interacts with FBP2; the interaction blocks FBP2 inhibition by physiological concentrations of AMP and reduces inhibition by Ca(2+)
Cytoplasm, myofibril, sarcomere, I band, Cytoplasm, myofibril, sarcomere, M line
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5TLE | X-ray | 1.58 Å | A/B/C/D=2-364 |
| 3BV4 | X-ray | 1.7 Å | A=5-344 |
| 1ZAI | X-ray | 1.76 Å | A/B/C/D=2-364 |
| 1ZAH | X-ray | 1.8 Å | A/B/C/D=2-364 |
| 3DFQ | X-ray | 1.82 Å | A/B/C/D=2-364 |
| 5F4X | X-ray | 1.84 Å | A/B/C/D=2-364 |
| 3DFN | X-ray | 1.86 Å | A/B/C/D=2-364 |
| 2QUT | X-ray | 1.88 Å | A/B/C/D=2-364 |
| 1ZAJ | X-ray | 1.89 Å | A/B/C/D=2-364 |
| 1ZAL | X-ray | 1.89 Å | A/B/C/D=2-364 |
| 1ADO | X-ray | 1.9 Å | A/B/C/D=2-364 |
| 3DFO | X-ray | 1.94 Å | A/B/C/D=2-364 |
| 3DFT | X-ray | 1.94 Å | A/B/C/D=2-364 |
| 11NU | EM | 1.97 Å | A/B/C/D=3-345 |
| 5TLZ | X-ray | 1.97 Å | A/B/C/D=2-364 |
| 11NX | EM | 1.98 Å | A/B/C/D=3-345 |
| 2QUU | X-ray | 1.98 Å | A/B/C/D=2-364 |
| 3B8D | X-ray | 2.0 Å | A/B/C/D=2-364 |
| 3DFS | X-ray | 2.03 Å | A/B/C/D=2-364 |
| 2OT0 | X-ray | 2.05 Å | A/B/C/D=2-364 |
Showing 20 of 60 experimental structures (best resolution first).
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