Q9UI10: Translation initiation factor eIF2B subunit delta (EIF2B4)

Translation initiation factor eIF2B subunit delta (EIF2B4) is a 523-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UI10.

Gene
EIF2B4
Organism
Homo sapiens
Length
523 residues
Mean pLDDT
76.5
Model
AF-Q9UI10-F1 v6
Model created
1 Aug 2025
PDB structures
25

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Model confidence (pLDDT)

The mean pLDDT of this model is 76.5 (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 accurate50%
70 to 90Confident: backbone generally right22%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions21%

What pLDDT means and how to read it

Function

Acts as a component of the translation initiation factor 2B (eIF2B) complex, which catalyzes the exchange of GDP for GTP on eukaryotic initiation factor 2 (eIF2) gamma subunit (PubMed:25858979, PubMed:27023709, PubMed:31048492). Its guanine nucleotide exchange factor activity is repressed when bound to eIF2 complex phosphorylated on the alpha subunit, thereby limiting the amount of methionyl-initiator methionine tRNA available to the ribosome and consequently global translation is repressed (PubMed:25858979, PubMed:31048492)

Subunit structure

Component of the translation initiation factor 2B (eIF2B) complex which is a heterodecamer of two sets of five different subunits: alpha, beta, gamma, delta and epsilon. Subunits alpha, beta and delta comprise a regulatory subcomplex and subunits epsilon and gamma comprise a catalytic subcomplex (PubMed:25858979, PubMed:27023709, PubMed:31048492). Within the complex, the hexameric regulatory…

Subcellular location

Cytoplasm, cytosol

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9ZUZX-ray2.25 ÅD=164-523
7VLKEM2.27 ÅG/H=1-523
7F64EM2.42 ÅG/H=1-523
7RLOEM2.6 ÅE/F=1-523
9HVEEM2.7 ÅG/H=1-523
7F66EM2.76 ÅG/H=1-523
6CAJEM2.8 ÅE/F=1-523
7L70EM2.8 ÅE/F=1-523
7TRJEM2.8 ÅE/F=1-523
8TQZEM2.9 ÅE/F=1-523
7KMFEM2.91 ÅE/F=1-523
7L7GEM3.0 ÅE/F=1-523
6O85EM3.03 ÅE/F=1-523
6O9ZEM3.03 ÅE/F=1-523
9HVDEM3.04 ÅG/H=1-523
8TQOEM3.1 ÅE=1-523
6O81EM3.21 ÅE/F=1-523
7F67EM3.59 ÅG/H=1-523
7D45EM3.8 ÅG/H=1-523
7D44EM4.0 ÅG/H=1-523

Showing 20 of 25 experimental structures (best resolution first).

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