Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a 335-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P04406.
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The mean pLDDT of this model is 98.1 (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 | 99% |
| 70 to 90 | Confident: backbone generally right | 1% |
| 50 to 70 | Low: treat with caution | 0% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Catalyzes the conversion of D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate in glycolysis and the reverse reaction in gluconeogenesis (PubMed:11724794, PubMed:3170585). Also shows nitrosylase activity, thereby playing a role in nuclear functions (PubMed:11724794, PubMed:3170585). Modulates the organization and assembly of the cytoskeleton (By similarity). Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation…
Homotetramer (PubMed:16239728, PubMed:16510976). Interacts with TPPP; the interaction is direct (By similarity). Interacts (when S-nitrosylated) with SIAH1; leading to nuclear translocation (By similarity). Interacts with RILPL1/GOSPEL, leading to prevent the interaction between GAPDH and SIAH1 and prevent nuclear translocation (By similarity). Interacts with CHP1; the interaction increases the…
Cytoplasm, cytosol, Nucleus, Cytoplasm, perinuclear region, Membrane, Cytoplasm, cytoskeleton
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6YND | X-ray | 1.52 Å | A/B/C/D/E/F/G/H=1-335 |
| 1U8F | X-ray | 1.75 Å | O/P/Q/R=1-335 |
| 9L3E | X-ray | 1.77 Å | O/P/Q/R=1-335 |
| 6M61 | X-ray | 1.82 Å | O/P/Q/R=1-335 |
| 8P5F | X-ray | 1.82 Å | AAA/DDD/EEE/GGG=1-335 |
| 6YNE | X-ray | 1.85 Å | A/B/C/D=1-335 |
| 8G17 | EM | 1.98 Å | A/B/C/D=2-335 |
| 4WNC | X-ray | 1.99 Å | A/B/C/D/E/F/G/O=1-335 |
| 8G15 | EM | 2.07 Å | A/B/C/D=2-335 |
| 8G16 | EM | 2.07 Å | A/B/C/D=2-335 |
| 8G12 | EM | 2.17 Å | A/B/C/D=2-335 |
| 6IQ6 | X-ray | 2.29 Å | A/B/C/D/E/F/G/H=1-335 |
| 4WNI | X-ray | 2.3 Å | A/B/C/O=1-335 |
| 8G13 | EM | 2.3 Å | A/B/C/D=2-335 |
| 8G14 | EM | 2.3 Å | A/B/C/D=2-335 |
| 6YNF | X-ray | 2.39 Å | A/B/C/D/E/F/G/H=2-335 |
| 1ZNQ | X-ray | 2.5 Å | O/P/Q/R=1-335 |
| 6YNH | X-ray | 2.62 Å | B/D/F/G=1-335 |
| 6ADE | X-ray | 3.15 Å | A/B/C=1-335 |
| 8DNS | EM | 3.22 Å | O/P/Q/R=1-335 |
Showing 20 of 21 experimental structures (best resolution first).
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