P18074: General transcription and DNA repair factor IIH helicase subunit XPD (ERCC2)

General transcription and DNA repair factor IIH helicase subunit XPD (ERCC2) is a 760-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P18074.

Gene
ERCC2
Organism
Homo sapiens
Length
760 residues
Mean pLDDT
87.6
Model
AF-P18074-F1 v6
Model created
1 Aug 2025
PDB structures
51

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Model confidence (pLDDT)

The mean pLDDT of this model is 87.6 (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 accurate54%
70 to 90Confident: backbone generally right41%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

ATP-dependent 5'-3' DNA helicase (PubMed:31253769, PubMed:8413672, PubMed:9771713). Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, not absolutely essential for minimal transcription in vitro (PubMed:10024882, PubMed:17466626, PubMed:9771713). Required for transcription-coupled nucleotide excision repair (NER) of damaged DNA; recognizes damaged bases (PubMed:17466626, PubMed:23352696, PubMed:9771713). Sequestered in chromatin on UV-damaged DNA (PubMed:23352696). When complexed to CDK-activating kinase (CAK), involved in transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged…

Subunit structure

Component of the 7-subunit TFIIH core complex composed of XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5, which is active in NER (PubMed:9771713, PubMed:9852112). The core complex associates with the 3-subunit CDK-activating kinase (CAK) module composed of CCNH/cyclin H, CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription (PubMed:9771713,…

Subcellular location

Nucleus, Cytoplasm, cytoskeleton, spindle

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6TUNX-ray2.07 ÅA/B=245-439
28JMEM3.29 ÅB=1-760
7EGBEM3.3 Å7=1-760
8EBUEM3.3 ÅB=1-760
9PD3EM3.3 ÅB=1-760
28JSEM3.32 ÅB=1-760
9PD4EM3.4 ÅB=1-760
6RO4EM3.5 ÅB=1-760
7AD8EM3.5 ÅB=1-760
9XYUEM3.5 ÅB=1-760
28KEEM3.6 ÅB=1-760
8EBXEM3.6 ÅB=1-760
8EBYEM3.6 ÅB=1-760
6NMIEM3.7 ÅB=1-760
7EGCEM3.9 Å7=1-760
7NVXEM3.9 Å0=1-760
8EBTEM3.9 ÅB=1-730
28JVEM3.91 ÅB=1-760
8BVWEM4.0 Å1=1-760
8EBSEM4.0 ÅB=1-760

Showing 20 of 51 experimental structures (best resolution first).

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