Bifunctional glutamate/proline--tRNA ligase (EPRS1) is a 1512-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P07814.
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The mean pLDDT of this model is 82.9 (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 | 52% |
| 70 to 90 | Confident: backbone generally right | 35% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 11% |
What pLDDT means and how to read it
Multifunctional protein which primarily functions within the aminoacyl-tRNA synthetase multienzyme complex, also known as multisynthetase complex. Within the complex it catalyzes the attachment of both L-glutamate and L-proline to their cognate tRNAs in a two-step reaction where the amino acid is first activated by ATP to form a covalent intermediate with AMP. Subsequently, the activated amino acid is transferred to the acceptor end of the cognate tRNA to form L-glutamyl-tRNA(Glu) and L-prolyl-tRNA(Pro) (PubMed:23263184, PubMed:24100331, PubMed:29576217, PubMed:3290852, PubMed:37212275). Upon interferon-gamma stimulation, EPRS1 undergoes phosphorylation, causing its dissociation from the…
Homodimer (PubMed:23263184, PubMed:24100331, PubMed:37212275). Part of the aminoacyl-tRNA synthetase multienzyme complex, also known as multisynthetase complex (MSC), that is composed of the tRNA ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), Leu (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase for Glu and Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and…
Cytoplasm, cytosol, Membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7X09 | X-ray | 1.7 Å | A/B=1008-1512 |
| 7F99 | X-ray | 1.98 Å | A/B=1008-1512 |
| 7Y1H | X-ray | 1.99 Å | A/B=1001-1512 |
| 4HVC | X-ray | 2.0 Å | A/B=1003-1512 |
| 7F98 | X-ray | 2.0 Å | A/B=1008-1512 |
| 7F9A | X-ray | 2.0 Å | A/B=1008-1512 |
| 7F9B | X-ray | 2.0 Å | A/B=1008-1512 |
| 7X1O | X-ray | 2.04 Å | A/B=1008-1512 |
| 5A1N | X-ray | 2.1 Å | A=1-175 |
| 7BBU | X-ray | 2.19 Å | A=1000-1512 |
| 7F9C | X-ray | 2.2 Å | A/B=1008-1512 |
| 7OSY | X-ray | 2.23 Å | A/B=1001-1512 |
| 7Y28 | X-ray | 2.29 Å | A/B=1016-1512 |
| 4K87 | X-ray | 2.3 Å | A=1000-1512 |
| 5A5H | X-ray | 2.32 Å | A/C/E/G=1-175 |
| 7OT0 | X-ray | 2.32 Å | A/B=1001-1512 |
| 5VAD | X-ray | 2.36 Å | A/B=998-1512 |
| 4K86 | X-ray | 2.4 Å | A=1000-1512 |
| 7OSZ | X-ray | 2.46 Å | A/B=1001-1512 |
| 7OT2 | X-ray | 2.48 Å | A/B=1001-1512 |
Showing 20 of 33 experimental structures (best resolution first).
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