P23025: DNA repair protein complementing XP-A cells (XPA)

DNA repair protein complementing XP-A cells (XPA) is a 273-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P23025.

Gene
XPA
Organism
Homo sapiens
Length
273 residues
Mean pLDDT
81.4
Model
AF-P23025-F1 v6
Model created
1 Aug 2025
PDB structures
18

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.4 (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 accurate51%
70 to 90Confident: backbone generally right21%
50 to 70Low: treat with caution18%
Below 50Very low: often disordered regions10%

What pLDDT means and how to read it

Function

Involved in DNA nucleotide excision repair (NER). Initiates repair by binding to damaged sites with various affinities, depending on the photoproduct and the transcriptional state of the region. Required for UV-induced CHEK1 phosphorylation and the recruitment of CEP164 to cyclobutane pyrimidine dimmers (CPD), sites of DNA damage after UV irradiation (PubMed:19197159). During NER stimulates the 5'-3' helicase activity of XPD/ERCC2 and the DNA translocase activity of XPB/ERCC3 (PubMed:31253769). Connects XPD/ERCC2 and XPB/ERCC3 during NER, retaining DNA near the XPB/ERCC3 active site, and stabilizing the complex in a different conformation than in transcribing TFIIH (PubMed:31253769)

Subunit structure

Interacts with GPN1. Interacts with RPA1 and RPA2; the interaction is direct and associates XPA with the RPA complex. Interacts (via N-terminus) with CEP164 upon UV irradiation. Interacts with HERC2. During NER binds XPD/ERCC2 and XPB/ERCC3 of transcription factor IIH (TFIIH), bridging the 2 proteins (PubMed:31253769)

Subcellular location

Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6J44X-ray2.06 ÅA=98-239
6LAEX-ray2.81 ÅA/B=98-239
9QECEM2.9 ÅC=1-273
8EBUEM3.3 ÅK=1-273
9PD3EM3.3 ÅK=1-273
9PD4EM3.4 ÅK=1-273
6RO4EM3.5 ÅG=1-273
7AD8EM3.5 ÅG=1-273
9XYUEM3.5 ÅK=1-273
28KEEM3.6 ÅN=1-273
8EBXEM3.6 ÅK=1-273
8EBYEM3.6 ÅK=1-273
8EBTEM3.9 ÅK=102-273
9PCPEM4.3 ÅK=1-273
9PD5EM5.7 ÅK=1-273
1D4UNMRA=98-208
1XPANMRA=98-219
2JNWNMRB=67-80

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