A0A1L8ENT6: Non-homologous end-joining factor 1 (nhej1.S)

Non-homologous end-joining factor 1 (nhej1.S) is a 297-residue protein from Xenopus laevis. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: A0A1L8ENT6.

Gene
nhej1.S
Organism
Xenopus laevis
Length
297 residues
Mean pLDDT
78.6
Model
AF-A0A1L8ENT6-F1 v6
Model created
1 Aug 2025
PDB structures
2

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 78.6 (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 accurate57%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions25%

What pLDDT means and how to read it

Function

DNA repair protein involved in DNA non-homologous end joining (NHEJ); required for double-strand break (DSB) repair and V(D)J recombination (PubMed:30177755, PubMed:33289484). It is also involved in telomere maintenance (By similarity). Plays a key role in NHEJ by promoting the ligation of various mismatched and non-cohesive ends (By similarity). In some studies, has been shown to associate with xrcc4 to form alternating helical filaments that bridge DNA and act like a bandage, holding together the broken DNA until it is repaired (By similarity). Alternatively, it has also been shown that rather than forming filaments, a single nhej1 dimer interacts through both head domains with xrcc4 to…

Subunit structure

Homodimer (PubMed:30177755). Interacts with xrcc4; the interaction is direct and is mediated via a head-to-head interaction between N-terminal head regions (PubMed:30177755). Component of the core long-range non-homologous end joining (NHEJ) complex (also named DNA-PK complex) composed of prkdc/DNA-PKcs, lig4, xrcc4, xrcc6/Ku70, xrcc5/Ku80 and nhej1/xlf (PubMed:33289484)

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6TYXX-ray1.9 ÅC/D=280-297
6TYTX-ray2.4 ÅB=280-297

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.