P61326: Protein mago nashi homolog (MAGOH)

Protein mago nashi homolog (MAGOH) is a 146-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P61326.

Gene
MAGOH
Organism
Homo sapiens
Length
146 residues
Mean pLDDT
93.8
Model
AF-P61326-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 93.8 (very high 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 accurate84%
70 to 90Confident: backbone generally right10%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Required for pre-mRNA splicing as component of the spliceosome (PubMed:11991638). Plays a redundant role with MAGOHB as core component of the exon junction complex (EJC) and in the nonsense-mediated decay (NMD) pathway (PubMed:23917022). The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream…

Subunit structure

Heterodimer with RBM8A (PubMed:12730685, PubMed:12781131, PubMed:23917022). Core component of the mRNA splicing-dependent exon junction complex (EJC); the core complex contains CASC3, EIF4A3, MAGOH or MAGOHB, and RBM8A (PubMed:11991638, PubMed:16170325, PubMed:16314458, PubMed:16923391, PubMed:16931718, PubMed:19033377, PubMed:20479275, PubMed:23917022). Component of the ALYREF/THOC4-EJC-RNA…

Subcellular location

Nucleus, Nucleus speckle, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1P27X-ray2.0 ÅA/C=2-145
2J0SX-ray2.21 ÅC=1-146
2HYIX-ray2.3 ÅA/G=1-146
3EX7X-ray2.3 ÅA/E=1-146
7ZNJEM2.4 ÅB/G/L/b/g/l=1-146
8C6JEM2.8 Å9=1-146
2J0QX-ray3.2 ÅC/F=1-146
9FMDEM3.3 Å9=1-146
2XB2X-ray3.4 ÅC/Y=1-146
8I0WEM3.4 Åv=1-146
7W59EM3.6 Åv=1-146
7W5AEM3.6 Åv=1-146
7W5BEM4.3 Åv=1-146
7A5PEM5.0 Åv=1-146

More AlphaFold highlights

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