Q15645: Pachytene checkpoint protein 2 homolog (TRIP13)

Pachytene checkpoint protein 2 homolog (TRIP13) is a 432-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15645.

Gene
TRIP13
Organism
Homo sapiens
Length
432 residues
Mean pLDDT
86.7
Model
AF-Q15645-F1 v6
Model created
1 Aug 2025
PDB structures
6

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 86.7 (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 accurate63%
70 to 90Confident: backbone generally right23%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions4%

What pLDDT means and how to read it

Function

Plays a key role in chromosome recombination and chromosome structure development during meiosis. Required at early steps in meiotic recombination that leads to non-crossovers pathways. Also needed for efficient completion of homologous synapsis by influencing crossover distribution along the chromosomes affecting both crossovers and non-crossovers pathways. Also required for development of higher-order chromosome structures and is needed for synaptonemal-complex formation. In males, required for efficient synapsis of the sex chromosomes and for sex body formation. Promotes early steps of the DNA double-strand breaks (DSBs) repair process upstream of the assembly of RAD51 complexes.…

Subunit structure

Specifically interacts with the ligand binding domain of the thyroid receptor (TR). This interaction does not require the presence of thyroid hormone for its interaction. Interacts with HPV16 E1. Interacts with proteasome subunit PSMA8; to participate in meiosis progression during spermatogenesis (By similarity)

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5WC2X-ray2.5 ÅA=1-432
5VQAX-ray2.54 ÅA=1-432
6LK0X-ray2.6 ÅA=1-432
5VQ9X-ray3.02 ÅD=1-432
7L9PEM3.6 ÅA/B/C/D/E/F=2-432
6F0XEM4.6 ÅA/B/C/D/E/F=1-432

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.