P15170: Eukaryotic peptide chain release factor GTP-binding subunit ERF3A (GSPT1)

Eukaryotic peptide chain release factor GTP-binding subunit ERF3A (GSPT1) is a 499-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P15170.

Gene
GSPT1
Organism
Homo sapiens
Length
499 residues
Mean pLDDT
81.8
Model
AF-P15170-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.8 (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 accurate49%
70 to 90Confident: backbone generally right36%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions14%

What pLDDT means and how to read it

Function

GTPase component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons UAA, UAG and UGA (PubMed:15987998, PubMed:19417105, PubMed:2511002, PubMed:27863242). GSPT1/ERF3A mediates ETF1/ERF1 delivery to stop codons: The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site (PubMed:27863242). GTP hydrolysis by GSPT1/ERF3A induces a conformational change that leads to its dissociation, permitting ETF1/ERF1 to accommodate fully in the A-site (PubMed:16777602, PubMed:27863242). Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD)…

Subunit structure

Component of the eRF1-eRF3-GTP ternary complex, composed of ETF1/ERF1 and ERF3 (GSPT1/ERF3A or GSPT2/ERF3B) and GTP (PubMed:19417105, PubMed:27863242). Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex (PubMed:19417104). The ETF1-GSPT1 complex interacts with JMJD4 (PubMed:24486019). Interacts with PABPC1 (By similarity). Interacts with SHFL (PubMed:30682371)

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3KUIX-ray2.3 ÅB=163-169
5HXBX-ray3.6 ÅA/X=300-496
6XK9X-ray3.64 ÅA/X=300-496
5LZTEM3.65 Åjj=1-499
3E1YX-ray3.8 ÅE/F/G/H=301-499
9HNEX-ray3.9 ÅA/D=300-496
4D61EM9.0 Åi=72-497
3J5YEM9.7 ÅB=69-496

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