Q02078: Myocyte-specific enhancer factor 2A (MEF2A)

Myocyte-specific enhancer factor 2A (MEF2A) is a 507-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q02078.

Gene
MEF2A
Organism
Homo sapiens
Length
507 residues
Mean pLDDT
54.7
Model
AF-Q02078-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 54.7 (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 accurate17%
70 to 90Confident: backbone generally right4%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions67%

What pLDDT means and how to read it

Function

Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation. Associates with chromatin to the ZNF16 promoter

Subunit structure

Binds DNA as a homo- or heterodimer. Dimerizes with MEF2D. Interacts with HDAC7 (By similarity). Interacts with PIAS1; the interaction enhances sumoylation. Interacts with HDAC4, HDAC9 and SLC2A4RG. Interacts (via the N-terminal) with MAPK7; the interaction results in the phosphorylation and transcriptional activity of MEF2A

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
1EGWX-ray1.5 ÅA/B/C/D=2-78
6WC2X-ray2.1 ÅA/B/C/D/I/J=9-72, A/B/C/D/I/J=92-95
3P57X-ray2.19 ÅA/B/C/D/I/J=2-91
1LEWX-ray2.3 ÅB=269-280
6BYYX-ray2.3 ÅA/B/C/D=1-64, A/B/C/D=92-95
3MU6X-ray2.43 ÅA/B/C/D=2-72
3KOVX-ray2.9 ÅA/B/I/J=2-91
6BZ1X-ray2.97 ÅA/B/C/D=1-64, A/B/C/D=92-95
7XUZX-ray3.59 ÅC/D/G/H=1-95
1C7UNMRA/B=2-86

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