Q01094: Transcription factor E2F1 (E2F1)

Transcription factor E2F1 (E2F1) is a 437-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q01094.

Gene
E2F1
Organism
Homo sapiens
Length
437 residues
Mean pLDDT
62.0
Model
AF-Q01094-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 62.0 (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 accurate23%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution20%
Below 50Very low: often disordered regions43%

What pLDDT means and how to read it

Function

Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication (PubMed:10675335, PubMed:12717439, PubMed:17050006, PubMed:17704056, PubMed:18625225, PubMed:28992046). The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase (PubMed:10675335, PubMed:12717439, PubMed:17704056). E2F1 binds preferentially RB1 in a cell-cycle dependent manner (PubMed:10675335, PubMed:12717439, PubMed:17704056). It can mediate both cell proliferation and TP53/p53-dependent apoptosis…

Subunit structure

Component of the DRTF1/E2F transcription factor complex. Forms heterodimers with DP family members. The E2F1 complex binds specifically hypophosphorylated RB1, the interaction represses E2F1-driven transcription (PubMed:8336704). During the cell cycle, RB1 becomes phosphorylated in mid-to-late G1 phase, detaches from the DRTF1/E2F complex, rendering E2F transcriptionally active. Viral…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6G0PX-ray1.3 ÅB=114-129
5M9OX-ray1.45 ÅB=108-116
6ULSX-ray1.5 ÅB=114-123
5M9NX-ray1.95 ÅC=104-120
1H24X-ray2.5 ÅE=87-95
2AZEX-ray2.55 ÅB=200-301
1O9KX-ray2.6 ÅP/Q/R/S=409-426
9CB3EM3.47 ÅC=84-96

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