Chaperonin GroEL (groEL) is a 548-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0A6F5.
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The mean pLDDT of this model is 90.8 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 76% |
| 70 to 90 | Confident: backbone generally right | 20% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding (PubMed:10532860, PubMed:16751100, PubMed:1676490, PubMed:18418386, PubMed:18987317, PubMed:20603018, PubMed:24816391, PubMed:2573517, PubMed:2897629, PubMed:8104102, PubMed:9285593). The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding, probably by preventing aggregation and by entropically destabilizing folding intermediates (PubMed:16751100, PubMed:18418386, PubMed:18987317, PubMed:20603018, PubMed:24816391). Rapid binding of ATP, followed by slower binding of…
Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back (PubMed:1361169, PubMed:15327959, PubMed:7935790, PubMed:8846220, PubMed:9285585). Interacts with the co-chaperonin GroES (PubMed:1361169, PubMed:25174333, PubMed:7638600, PubMed:7638601, PubMed:8618836, PubMed:8663256, PubMed:9285585). Can form asymmetrical complexes, composed of one GroEL and one GroES, and…
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3VZ6 | X-ray | 1.5 Å | A=190-376 |
| 1KID | X-ray | 1.7 Å | A=186-376 |
| 3VZ7 | X-ray | 1.8 Å | A=191-376 |
| 3VZ8 | X-ray | 1.9 Å | A/B/C=191-376 |
| 1KP8 | X-ray | 2.0 Å | A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548 |
| 1SX3 | X-ray | 2.0 Å | A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-526 |
| 1DK7 | X-ray | 2.02 Å | A/B=191-336 |
| 1LA1 | X-ray | 2.06 Å | A=188-379 |
| 1DKD | X-ray | 2.1 Å | A/B/C/D=191-336 |
| 1FY9 | X-ray | 2.2 Å | A=191-376 |
| 1FYA | X-ray | 2.2 Å | A=191-376 |
| 8BKZ | EM | 2.3 Å | A/BA/C/E/G/I/K/M/O/Q/S/V/X/Z=1-548 |
| 8BL2 | EM | 2.3 Å | A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548 |
| 8S32 | EM | 2.45 Å | A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548 |
| 1JON | X-ray | 2.5 Å | A=191-345 |
| 8BMT | EM | 2.5 Å | A/BA/C/E/G/I/J/L/N/P/R/T/X/Z=1-548 |
| 8P4M | EM | 2.5 Å | A/B/C/D/E/F/G=1-548 |
| 1SS8 | X-ray | 2.7 Å | A/B/C/D/E/F/G=2-525 |
| 7XOK | EM | 2.7 Å | A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548 |
| 8BLC | EM | 2.7 Å | A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548 |
Showing 20 of 94 experimental structures (best resolution first).
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