General transcription factor IIH subunit 2 (GTF2H2) is a 395-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13888.
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The mean pLDDT of this model is 84.3 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 53% |
| 70 to 90 | Confident: backbone generally right | 29% |
| 50 to 70 | Low: treat with caution | 13% |
| Below 50 | Very low: often disordered regions | 5% |
What pLDDT means and how to read it
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by…
Component of the TFIID-containing RNA polymerase II pre-initiation complex that is composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2 and ERCC3 (PubMed:27193682). 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. The core complex…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 28JM | EM | 3.29 Å | E=1-395 |
| 7EGB | EM | 3.3 Å | 2=1-395 |
| 8EBU | EM | 3.3 Å | E=1-395 |
| 9PD3 | EM | 3.3 Å | E=1-395 |
| 28JS | EM | 3.32 Å | E=1-395 |
| 5O85 | X-ray | 3.4 Å | B/D=1-395 |
| 9PD4 | EM | 3.4 Å | E=1-395 |
| 6RO4 | EM | 3.5 Å | D=1-395 |
| 7AD8 | EM | 3.5 Å | D=1-395 |
| 9XYU | EM | 3.5 Å | E=1-395 |
| 28KE | EM | 3.6 Å | E=1-395 |
| 8EBX | EM | 3.6 Å | E=1-395 |
| 8EBY | EM | 3.6 Å | E=1-395 |
| 6NMI | EM | 3.7 Å | E=51-387 |
| 7EGC | EM | 3.9 Å | 2=1-395 |
| 7NVX | EM | 3.9 Å | 6=1-395 |
| 8EBT | EM | 3.9 Å | E=8-387 |
| 28JV | EM | 3.91 Å | E=1-395 |
| 8BVW | EM | 4.0 Å | 4=1-395 |
| 8EBS | EM | 4.0 Å | E=1-395 |
Showing 20 of 52 experimental structures (best resolution first).
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