P81795: Eukaryotic translation initiation factor 2 subunit 3, X-linked (Eif2s3)

Eukaryotic translation initiation factor 2 subunit 3, X-linked (Eif2s3) is a 472-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P81795.

Gene
Eif2s3
Organism
Rattus norvegicus
Length
472 residues
Mean pLDDT
84.3
Model
AF-P81795-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.3 (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 accurate34%
70 to 90Confident: backbone generally right59%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

Member of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. 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 eIF-2B (By similarity). Along with its paralog on chromosome Y, may contribute to spermatogenesis up to the round…

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. eIF2 is member of the 43S pre-initiation complex (43S PIC). Interacts (via C-terminus) with CDC123; the interaction is direct

Subcellular location

Cytoplasm, cytosol

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9H6YEM2.9 ÅB=1-472

More AlphaFold highlights

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