P23301: Eukaryotic translation initiation factor 5A-1 (HYP2)

Eukaryotic translation initiation factor 5A-1 (HYP2) is a 157-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P23301.

Gene
HYP2
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
157 residues
Mean pLDDT
88.1
Model
AF-P23301-F1 v6
Model created
1 Aug 2025
PDB structures
20

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Model confidence (pLDDT)

The mean pLDDT of this model is 88.1 (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 accurate78%
70 to 90Confident: backbone generally right11%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions8%

What pLDDT means and how to read it

Function

Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (PubMed:10229683, PubMed:16157662, PubMed:16914118, PubMed:19338753, PubMed:19424157, PubMed:23727016, PubMed:24923804, PubMed:28392174, PubMed:36804914, PubMed:641056, PubMed:8307948, PubMed:9582285). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome (PubMed:23727016, PubMed:24923804, PubMed:28392174). Acts as a ribosome quality control (RQC) cofactor by…

Subunit structure

Homodimer (PubMed:19120453). Binds to 80S ribosomes (PubMed:16215987, PubMed:27115996). Actively translating ribosomes show mutually exclusive binding of eIF5a (HYP2 or ANB1) and EFT1/eEF2 (PubMed:27115996). Interacts with DYS1 and LIA1 (PubMed:14675757, PubMed:16215987)

Subcellular location

Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8AGXEM2.4 Åv=1-157
8BN3EM2.4 ÅeI=10-154
8AAFEM2.5 Åv=1-157
8AGTEM2.6 Åv=1-157
8AGVEM2.6 Åv=1-157
8AGZEM2.6 Åv=1-157
8AGUEM2.7 Åv=1-157
6TNUEM3.1 ÅeI=4-157
5DATX-ray3.15 Åf=1-157
8K2DEM3.2 ÅCE=1-157
8UT0EM3.22 ÅLs=1-157
5DC3X-ray3.25 Åf=1-157
5DGFX-ray3.3 Åf=1-157
3ER0X-ray3.35 ÅA/B=1-157
5DGEX-ray3.45 Åf=1-157
8Y0UEM3.59 Å5=1-157
6Q84X-ray3.7 ÅC/F=16-157
5MC6EM3.8 ÅBT=1-157
5GAKEM3.88 Åq=1-157
7NRCEM3.9 ÅLs=4-157

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