P20226: TATA-box-binding protein (TBP)

TATA-box-binding protein (TBP) is a 339-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P20226.

Gene
TBP
Organism
Homo sapiens
Length
339 residues
Mean pLDDT
77.1
Model
AF-P20226-F1 v6
Model created
1 Aug 2025
PDB structures
77

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 77.1 (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 accurate52%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions24%

What pLDDT means and how to read it

Function

The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:2194289, PubMed:2363050, PubMed:2374612, PubMed:27193682, PubMed:33795473). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:27007846, PubMed:33795473). The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C…

Subunit structure

Binds DNA as monomer (PubMed:2194289, PubMed:2374612). Component of the TFIID basal transcription factor complex, composed of TATA-box-binding protein TBP, and a number of TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:27007846, PubMed:33795473, PubMed:9836642). Part of a TFIID-containing RNA polymerase II…

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
1CDWX-ray1.9 ÅA=159-337
4ROCX-ray1.9 ÅB=159-339
1NVPX-ray2.1 ÅA=159-339
4ROEX-ray2.2 ÅB=159-339
7NVUEM2.5 ÅO=1-339
1JFIX-ray2.62 ÅC=159-339
1C9BX-ray2.65 ÅB/F/J/N/R=158-337
4RODX-ray2.7 ÅB=159-339
5N9GX-ray2.7 ÅB/G=159-339
7NVSEM2.8 ÅO=1-339
1TGHX-ray2.9 ÅA=155-339
7NVTEM2.9 ÅO=1-339
8S52EM2.9 ÅO=1-339
7ZWDEM3.0 ÅO=1-339
7ZX8EM3.0 ÅO=1-339
9K3UEM3.0 ÅU=1-339
8S51EM3.1 ÅO=1-339
7EGFEM3.16 ÅP=1-339
7ZWCEM3.2 ÅO=1-339
9FSOEM3.28 ÅR=159-339

Showing 20 of 77 experimental structures (best resolution first).

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.