P68104: Elongation factor 1-alpha 1 (EEF1A1)

Elongation factor 1-alpha 1 (EEF1A1) is a 462-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P68104.

Gene
EEF1A1
Organism
Homo sapiens
Length
462 residues
Mean pLDDT
88.1
Model
AF-P68104-F1 v6
Model created
1 Aug 2025
PDB structures
13

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Model confidence (pLDDT)

The mean pLDDT of this model is 88.1 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate59%
70 to 90Confident: backbone generally right36%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond…

Subunit structure

Found in a nuclear export complex with XPO5, EEF1A1, Ran and aminoacylated tRNA (PubMed:12426392, PubMed:12426393). Interacts with PARP1 (PubMed:17177976). Interacts with KARS1 (PubMed:18029264). May interact with ERGIC2 (PubMed:17980171). Interacts with IFIT1 (via TPR repeats 4-7) (By similarity). Interacts with DLC1, facilitating distribution to the membrane periphery and ruffles upon growth…

Subcellular location

Cytoplasm, Nucleus, Nucleus, nucleolus, Cell membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
3C5JX-ray1.8 ÅC=343-355
9P8BEM2.48 ÅCF=4-444
8G60EM2.54 ÅEF=1-462
9P7OEM2.65 ÅCF=4-444
9PA7EM2.67 ÅCF=4-444
8G6JEM2.8 ÅEF=1-462
9P7KEM2.8 ÅCF=4-444
9P76EM2.83 ÅCF=4-444
9P7NEM2.83 ÅCF=4-444
9P7LEM2.92 ÅCF=4-444
6ZMOEM3.1 ÅCD=1-462
9P7HEM3.68 ÅCF=4-444
9P7IEM3.69 ÅCF=4-444

More AlphaFold highlights

About this viewer

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