P15336: Cyclic AMP-dependent transcription factor ATF-2 (ATF2)

Cyclic AMP-dependent transcription factor ATF-2 (ATF2) is a 505-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P15336.

Gene
ATF2
Organism
Homo sapiens
Length
505 residues
Mean pLDDT
57.8
Model
AF-P15336-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 57.8 (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 accurate13%
70 to 90Confident: backbone generally right12%
50 to 70Low: treat with caution25%
Below 50Very low: often disordered regions50%

What pLDDT means and how to read it

Function

Transcriptional activator which regulates the transcription of various genes, including those involved in anti-apoptosis, cell growth, and DNA damage response (PubMed:11932306, PubMed:15105425, PubMed:15916964, PubMed:22304920, PubMed:2529117). Dependent on its binding partner, binds to CRE (cAMP response element) consensus sequences (5'-TGACGTCA-3') or to AP-1 (activator protein 1) consensus sequences (5'-TGACTCA-3') (PubMed:11932306, PubMed:2529117). In the nucleus, contributes to global transcription and the DNA damage response, in addition to specific transcriptional activities that are related to cell development, proliferation and death (PubMed:22304920). In liver, acts as a…

Subunit structure

Binds DNA as a dimer and can form a homodimer in the absence of DNA (PubMed:11932306, PubMed:2529117). Can form a heterodimer with JUN (PubMed:22275354). Heterodimerization is essential for its transcriptional activity (PubMed:22275354). Binds through its N-terminal region to UTF1 which acts as a coactivator of ATF2 transcriptional activity (PubMed:9748258). Interacts with the HK1/VDAC1 complex…

Subcellular location

Nucleus, Cytoplasm, Mitochondrion outer membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6ZQSX-ray1.95 ÅB=83-102
8YPEX-ray1.95 ÅB=46-80
8YPFX-ray2.0 ÅB=46-90
9Y0RX-ray2.2 ÅB=352-378
6ZR5X-ray2.7 ÅC/D=20-58
1T2KX-ray3.0 ÅD=354-414
4H36X-ray3.0 ÅB=48-55
1BHINMRA=19-56

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