P06733: Alpha-enolase (ENO1)

Alpha-enolase (ENO1) is a 434-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P06733.

Gene
ENO1
Organism
Homo sapiens
Length
434 residues
Mean pLDDT
97.6
Model
AF-P06733-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 97.6 (very high 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 accurate98%
70 to 90Confident: backbone generally right2%
50 to 70Low: treat with caution0%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Enolase that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate in glycolysis and the reverse reaction in gluconeogenesis (PubMed:1369209, PubMed:29775581). Also involved in various processes such as growth control, hypoxia tolerance and allergic responses (PubMed:10802057, PubMed:12666133, PubMed:2005901, PubMed:29775581). May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons (PubMed:12666133). Stimulates immunoglobulin production (PubMed:1369209)

Subunit structure

Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific (PubMed:18560153). ENO1 interacts with PLG in the neuronal plasma membrane and promotes its activation. The C-terminal lysine is required for this binding (PubMed:9308760). Isoform MBP-1 interacts with TRAPPC2B (PubMed:11134351).…

Subcellular location

Cytoplasm, Cell membrane, Cytoplasm, myofibril, sarcomere, M line, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5NI9X-ray1.33 ÅC=326-340
5NIGX-ray1.35 ÅC=326-340
5OCKX-ray1.6 ÅA=5-21
5JLZX-ray1.99 ÅE/F=26-40
2PSNX-ray2.2 ÅA/B/C/D=1-434
3B97X-ray2.2 ÅA/B/C/D=2-434
8TRLX-ray2.4 ÅC/F=10-22
5LAXX-ray2.6 ÅE/F=26-40

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