Glucose-6-phosphate 1-dehydrogenase (G6PD) is a 515-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P11413.
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The mean pLDDT of this model is 94.4 (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 | 91% |
| 70 to 90 | Confident: backbone generally right | 3% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis. Also catalyzes the conversion of NAADPH, which is produced by enzymes such as DUOX1, DUOX2 and NOX5 from NAADP and promotes Ca(2+) signaling during T cell activation, back to NAADP (PubMed:34784249)
Homotetramer; dimer of dimers (PubMed:10745013, PubMed:15858258, PubMed:24769394, PubMed:38066190). Interacts with SIRT2; the interaction is enhanced by H(2)O(2) treatment (PubMed:24769394). Forms a ternary complex with ALDOB and TP53; this interaction is direct. ALDOB stabilizes the complex inhibiting G6PD activity and keeping oxidative pentose phosphate metabolism in check
Cytoplasm, cytosol, Membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6JYU | X-ray | 1.89 Å | A=29-513 |
| 6E08 | X-ray | 1.9 Å | L=1-515 |
| 7SNH | EM | 2.2 Å | A/B/C/D=1-515 |
| 7ZVE | X-ray | 2.28 Å | A=5-505, B=6-503, C/F=7-503, D/H=5-503, E=5-504, G=8-503 |
| 7ZVD | X-ray | 2.46 Å | N=28-511 |
| 2BH9 | X-ray | 2.5 Å | A=27-515 |
| 7SNI | EM | 2.5 Å | A/B/C/D=1-515 |
| 7UC2 | EM | 2.5 Å | A/B/C/D=1-515 |
| 6E07 | X-ray | 2.6 Å | B/C/F/L/N/Q/T/W=1-515 |
| 5UKW | X-ray | 2.65 Å | A=29-511 |
| 7SNG | EM | 2.8 Å | A/B/C/D=1-515 |
| 2BHL | X-ray | 2.9 Å | A/B=28-515 |
| 7SEH | X-ray | 2.9 Å | A/B=1-515 |
| 7UAL | EM | 2.9 Å | A/B/C/D=1-515 |
| 6VAQ | X-ray | 2.95 Å | A=1-515 |
| 1QKI | X-ray | 3.0 Å | A/B/C/D/E/F/G/H=2-515 |
| 7TOE | EM | 3.0 Å | A/B/C/D=1-515 |
| 6VA7 | X-ray | 3.07 Å | A=1-515 |
| 6VA0 | X-ray | 3.1 Å | A=1-515 |
| 7SNF | EM | 3.4 Å | A/B=1-515 |
Showing 20 of 25 experimental structures (best resolution first).
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