O13539: THO complex subunit THP2 (THP2)

THO complex subunit THP2 (THP2) is a 261-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O13539.

Gene
THP2
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
261 residues
Mean pLDDT
71.1
Model
AF-O13539-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 71.1 (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 accurate2%
70 to 90Confident: backbone generally right66%
50 to 70Low: treat with caution17%
Below 50Very low: often disordered regions15%

What pLDDT means and how to read it

Function

Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing formation of DNA:RNA hybrids behind the elongating polymerase. It functions in cotranscriptional formation of an export-competent messenger ribonucleoprotein particle (mRNP) by facilitating the loading of ATP-dependent RNA helicase SUB2 and the mRNA export factor YRA1 along the nascent mRNA

Subunit structure

Component of the THO complex, which is composed of HPR1, MFT1, THO2 and THP2. Together with SUB2, TEX1 and YRA1, THO forms the transcription/export (TREX) complex. THO associates with DNA and RNA in vitro

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7V2WEM3.2 ÅJ=1-261
7APXEM3.4 ÅC=1-261
7V2YEM3.4 ÅE=1-261
7LUVEM3.7 ÅB=1-261
7AQOEM4.5 ÅC/J=1-261

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About this viewer

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