Q9BUH6: Protein PAXX (PAXX)

Protein PAXX (PAXX) is a 204-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9BUH6.

Gene
PAXX
Organism
Homo sapiens
Length
204 residues
Mean pLDDT
82.9
Model
AF-Q9BUH6-F1 v6
Model created
1 Aug 2025
PDB structures
20

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Model confidence (pLDDT)

The mean pLDDT of this model is 82.9 (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 accurate59%
70 to 90Confident: backbone generally right16%
50 to 70Low: treat with caution18%
Below 50Very low: often disordered regions7%

What pLDDT means and how to read it

Function

Non-essential DNA repair protein involved in DNA non-homologous end joining (NHEJ); participates in double-strand break (DSB) repair and V(D)J recombination (PubMed:25574025, PubMed:25670504, PubMed:25941166, PubMed:27705800). May act as a scaffold required for accumulation of the Ku heterodimer, composed of XRCC5/Ku80 and XRCC6/Ku70, at double-strand break sites and promote the assembly and/or stability of the NHEJ machinery (PubMed:25574025, PubMed:25670504, PubMed:25941166). Involved in NHEJ by promoting the ligation of blunt-ended DNA ends (PubMed:27703001). Together with NHEJ1/XLF, collaborates with DNA polymerase lambda (POLL) to promote joining of non-cohesive DNA ends…

Subunit structure

Homodimer (PubMed:25574025). Interacts with the DNA-bound XRCC5/Ku80 and XRCC6/Ku70 heterodimer (Ku complex); the interaction is direct (PubMed:25574025, PubMed:27601299, PubMed:27705800). Associated component of the non-homologous end joining (NHEJ) complex, composed of the core proteins PRKDC, LIG4, XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF (PubMed:25670504, PubMed:25941166). Interacts with…

Subcellular location

Nucleus, Chromosome, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3WTDX-ray2.35 ÅA/B=1-166
4WJAX-ray2.6 ÅA/B=1-145
7ZYGEM2.68 ÅC=1-204
7ZWAEM2.8 ÅC=1-204
9CQ3EM2.8 ÅG/H=1-204
9GYFEM2.8 ÅC=180-202
9N81EM2.8 ÅG/H=1-204
8ASCX-ray2.95 ÅJ/T=177-204
9CQ6EM3.1 ÅG/H=1-204
9N83EM3.1 ÅG/H=1-204
9N82EM3.3 ÅG/H=1-204
9CQCEM3.4 ÅG/H=1-204
3WTFX-ray3.45 ÅA/B=1-204
9GD7EM4.25 ÅM=1-204
8EZAEM4.39 ÅS/T=1-204
8BHVEM4.51 Åc/i=1-204
8BH3EM4.55 ÅD/M=1-204
9G9LEM4.63 ÅM=1-204
8BHYEM5.33 ÅD/M=1-204
8EZBEM8.9 ÅS/T=1-204

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