Co-chaperonin GroES (groES) is a 97-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0A6F9.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 88.4 (confident 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 | 66% |
| 70 to 90 | Confident: backbone generally right | 20% |
| 50 to 70 | Low: treat with caution | 14% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Together with the chaperonin GroEL, 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). 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). GroES binds to the apical surface of the GroEL ring, thereby capping the opening of…
Heptamer of 7 subunits arranged in a ring (PubMed:1361169, PubMed:9285585). Interacts with the chaperonin GroEL (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 symmetrical complexes, formed between one GroEL and two GroES oligomers (PubMed:1361169,…
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8BKZ | EM | 2.3 Å | AA/B/CA/D/F/H/J/L/N/P/R/T/W/Y=2-97 |
| 8BMT | EM | 2.5 Å | AA/B/CA/D/F/H/K/M/O/Q/S/V/W/Y=2-97 |
| 8P4M | EM | 2.5 Å | O/P/Q/R/S/T/U=1-97 |
| 8BM1 | EM | 2.7 Å | B/E/J/M/P/S/W=2-97 |
| 1PCQ | X-ray | 2.81 Å | O/P/Q/R/S/T/U=1-97 |
| 1SVT | X-ray | 2.81 Å | O/P/Q/R/S/T/U=1-97 |
| 8P4N | EM | 2.9 Å | O/P/Q/R/S/T/U=1-97 |
| 8QXT | EM | 2.9 Å | O/P/Q/R/S/T/U=1-97 |
| 1PF9 | X-ray | 2.99 Å | O/P/Q/R/S/T/U=1-97 |
| 1AON | X-ray | 3.0 Å | O/P/Q/R/S/T/U=1-97 |
| 1SX4 | X-ray | 3.0 Å | O/P/Q/R/S/T/U=1-97 |
| 8P4O | EM | 3.04 Å | O/P/Q/R/S/T/U=1-97 |
| 8QXS | EM | 3.12 Å | O/P/Q/R/S/T/U=1-97 |
| 7PBJ | EM | 3.4 Å | Af/Am/At/Ba/Bh/Bo/Bv=1-97 |
| 8BM0 | EM | 3.4 Å | B/E/J/M/P/S/W=2-97 |
| 8BMO | EM | 3.4 Å | D/G/K/N/Q/T/W=2-97 |
| 7PBX | EM | 3.43 Å | Af/Al/Ar/Ax/Bd/Bj/Bp=1-97 |
| 5OPX | X-ray | 3.64 Å | 1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-97 |
| 8BA9 | EM | 3.7 Å | O/P/Q/R/S/T/U=1-97 |
| 3WVL | X-ray | 3.79 Å | O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b=1-97 |
Showing 20 of 31 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.