P49842: Winged helix repair factor 1 (WHR1)

Winged helix repair factor 1 (WHR1) is a 254-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P49842.

Gene
WHR1
Organism
Homo sapiens
Length
254 residues
Mean pLDDT
87.4
Model
AF-P49842-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 87.4 (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 accurate81%
70 to 90Confident: backbone generally right5%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions11%

What pLDDT means and how to read it

Function

DNA-binding protein which is required for efficient transcription-coupled nucleotide excision repair (TC-NER) (PubMed:38252411, PubMed:38890355, PubMed:39353615, PubMed:39547223, PubMed:39547228, PubMed:39547229). Acts as part of a TC-NER complex which assembles and interacts with RNA polymerase II (RNAPII) when it stalls at DNA lesions (PubMed:39547223, PubMed:39547228, PubMed:39547229). TC-NER complex subunit UVSSA binds to the GTF2H1/p62 subunit of the TFIIH transcription factor complex, tethering TFIIH to the TC-NER complex (PubMed:39547228). WHR1/STK19 then interacts with the XPD helicase subunit of TFIIH which guides TFIIH to DNA downstream of the stalled RNAPII, ensuring DNA repair…

Subunit structure

Monomer in solution (PubMed:38890355). Homodimer; when bound to DNA (PubMed:38252411). Component of a transcription-coupled nucleotide excision repair (TC-NER) complex composed of STK19, ERCC6, ERCC8, DDA1, DDB1, ELOF1 and UVSSA which assembles and interacts with the multiprotein RNA polymerase II complex when it stalls at DNA lesions (PubMed:39547223, PubMed:39547228, PubMed:39547229)

Subcellular location

Nucleus, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8YCMX-ray1.32 ÅA/B=31-254
7XRBX-ray1.65 ÅA/B=25-254
9BZ0EM1.9 Åf=1-254
9ER2EM3.3 ÅQ=1-254
9FD2EM3.4 Åg=1-254

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