ATPase GET3 (GET3) is a 354-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q12154.
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The mean pLDDT of this model is 83.0 (confident 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 | 48% |
| 70 to 90 | Confident: backbone generally right | 34% |
| 50 to 70 | Low: treat with caution | 15% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1 and GET2, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-GET2…
Homodimer. Component of the Golgi to ER traffic (GET) complex, which is composed of GET1, GET2 and GET3. Within the complex, GET1 and GET2 form a heterotetramer which is stabilized by phosphatidylinositol binding and which binds to the GET3 homodimer (PubMed:32910895). Interacts with the chloride channel protein GEF1
Cytoplasm, Endoplasmic reticulum, Golgi apparatus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2WOJ | X-ray | 1.99 Å | A/B/C/D=1-354 |
| 4XTR | X-ray | 2.05 Å | A/B=1-354 |
| 3ZS9 | X-ray | 2.1 Å | A/B=1-354 |
| 3H84 | X-ray | 2.3 Å | A/B=1-354 |
| 4XVU | X-ray | 2.35 Å | A/B/G/H=1-354 |
| 4XWO | X-ray | 2.75 Å | A/B/G/H/M/N/S/T=1-354 |
| 3A36 | X-ray | 2.8 Å | A/B=1-354 |
| 5BW8 | X-ray | 2.8 Å | A/B=2-354 |
| 3A37 | X-ray | 3.0 Å | A/B=1-354 |
| 3B2E | X-ray | 3.0 Å | A/B/C/D=1-354 |
| 3SJA | X-ray | 3.0 Å | A/B/E/F/I=1-354 |
| 3ZS8 | X-ray | 3.0 Å | A/B=1-354 |
| 9NS5 | EM | 3.19 Å | A/D=1-354 |
| 3SJC | X-ray | 3.2 Å | A/B/E/F=1-354 |
| 3SJB | X-ray | 3.3 Å | A/B=1-354 |
| 3IDQ | X-ray | 3.7 Å | A=1-354 |
| 3VLC | X-ray | 4.5 Å | A=1-354 |
| 3SJD | X-ray | 4.6 Å | A/B/C=1-354 |
| 4PWX | X-ray | 5.4 Å | A/B=2-354 |
| 5BWK | X-ray | 6.0 Å | A/B/C/D/M/N/O/P=2-354 |
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