P20042: Eukaryotic translation initiation factor 2 subunit 2 (EIF2S2)

Eukaryotic translation initiation factor 2 subunit 2 (EIF2S2) is a 333-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P20042.

Gene
EIF2S2
Organism
Homo sapiens
Length
333 residues
Mean pLDDT
64.9
Model
AF-P20042-F1 v6
Model created
1 Aug 2025
PDB structures
13

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Model confidence (pLDDT)

The mean pLDDT of this model is 64.9 (low 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 accurate26%
70 to 90Confident: backbone generally right20%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions42%

What pLDDT means and how to read it

Function

Component of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (PubMed:31836389). This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form the 43S pre-initiation complex (43S PIC). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF2B (By similarity)

Subunit structure

Eukaryotic translation initiation factor 2 eIF2 is a heterotrimeric complex composed of an alpha (EIF2S1), a beta (EIF2S2) and a gamma (EIF2S3) chain (PubMed:23063529, PubMed:31048492, PubMed:31836389, PubMed:35031321). eIF2 is member of the 43S pre-initiation complex (43S PIC). eIF2 forms a complex with at least CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (By similarity).…

Subcellular location

Cytoplasm, cytosol

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8PPLEM2.65 ÅIs=1-333
9HVEEM2.7 ÅM/N=1-333
6ZP4EM2.9 Å4=1-333
8PJ1EM3.4 Ås=1-333
7A09EM3.5 Å4=1-333
8OZ0EM3.5 ÅU=1-333
6ZMWEM3.7 Ås=1-333
6YBVEM3.8 Ås=1-333
9HVFEM3.8 ÅC=1-333
6K71EM4.3 ÅM=1-333
7D43EM4.3 ÅM=1-333
6K72EM4.6 ÅM=1-333
7QP6EM4.7 Ås=1-333

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