Q04637: Eukaryotic translation initiation factor 4 gamma 1 (EIF4G1)

Eukaryotic translation initiation factor 4 gamma 1 (EIF4G1) is a 1599-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q04637.

Gene
EIF4G1
Organism
Homo sapiens
Length
1599 residues
Mean pLDDT
55.0
Model
AF-Q04637-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 55.0 (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 accurate12%
70 to 90Confident: backbone generally right24%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions55%

What pLDDT means and how to read it

Function

Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:29987188). Exists in two complexes, either with EIF1 or with EIF4E (mutually exclusive) (PubMed:29987188). Together with EIF1, is required for leaky scanning, in particular for avoiding cap-proximal start codon (PubMed:29987188). Together with EIF4E, antagonizes the scanning promoted by EIF1-EIF4G1 and locates the start codon (through a TISU element) without scanning (PubMed:29987188). As a member of the eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 mRNA translation…

Subunit structure

eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E (cap-binding) and EIF4G1/EIF4G3 (PubMed:7651417, PubMed:7935836, PubMed:9372926). Interacts with eIF3 complex, mutually exclusive with EIF4A1 or EIF4A2, EIF4E and through its N-terminus with PABPC1 (PubMed:10970864, PubMed:10996799,…

Subcellular location

Cytoplasm, Nucleus, Cytoplasm, Stress granule

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5T46X-ray1.53 ÅB/D=592-653
5EI3X-ray1.71 ÅB=609-622
4F02X-ray2.0 ÅC/F=178-203
4AZAX-ray2.16 ÅB/D=609-620
1UG3X-ray2.24 ÅA/B=1233-1571
5ZK5X-ray2.25 ÅB=609-623
2W97X-ray2.29 ÅE/F=609-622
1LJ2X-ray2.38 ÅC/D=172-199
5EHCX-ray2.4 ÅB=609-622
5EIRX-ray2.69 ÅB=609-622
8OZ0EM3.5 Å2=197-1599
6ZMWEM3.7 Åg=290-1599
8J7REM3.7 ÅB=746-992
8HUJEM3.76 ÅB=746-992

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