Q6ZYL4: General transcription factor IIH subunit 5 (GTF2H5)

General transcription factor IIH subunit 5 (GTF2H5) is a 71-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q6ZYL4.

Gene
GTF2H5
Organism
Homo sapiens
Length
71 residues
Mean pLDDT
68.9
Model
AF-Q6ZYL4-F1 v6
Model created
1 Aug 2025
PDB structures
53

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Model confidence (pLDDT)

The mean pLDDT of this model is 68.9 (low 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 accurate0%
70 to 90Confident: backbone generally right62%
50 to 70Low: treat with caution28%
Below 50Very low: often disordered regions10%

What pLDDT means and how to read it

Function

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…

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. 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:15220921). Part of TBP-based Pol II…

Subcellular location

Nucleus, Cytoplasm

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1YDLX-ray2.3 ÅA=6-71
7NVVEM2.9 Å5=1-71
28JMEM3.29 ÅG=1-71
7EGBEM3.3 Å5=1-71
8EBUEM3.3 ÅG=1-71
9PD3EM3.3 ÅG=1-71
28JSEM3.32 ÅG=1-71
9PD4EM3.4 ÅG=1-71
6RO4EM3.5 ÅF=1-71
7AD8EM3.5 ÅF=1-71
9XYUEM3.5 ÅG=1-71
28KEEM3.6 ÅG=1-71
8EBXEM3.6 ÅG=1-71
8EBYEM3.6 ÅG=1-71
6NMIEM3.7 ÅG=1-71
7EGCEM3.9 Å5=1-71
7NVXEM3.9 Å5=1-71
8EBTEM3.9 ÅG=4-69
28JVEM3.91 ÅG=1-71
8BVWEM4.0 Å6=1-71

Showing 20 of 53 experimental structures (best resolution first).

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