Chaperone protein ClpB (clpB) is a 848-residue protein from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P9WPD1.
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The mean pLDDT of this model is 87.8 (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 | 55% |
| 70 to 90 | Confident: backbone generally right | 39% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity)
Homohexamer. The oligomerization is ATP-dependent (By similarity)
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6W6G | EM | 3.1 Å | A/B/C/D/E/F=1-848 |
| 6W6J | EM | 3.2 Å | A/B/C/D/E/F=1-848 |
| 6W6H | EM | 3.3 Å | A/B/C/D/E/F=1-848 |
| 6W6I | EM | 3.5 Å | A/B/C/D/E/F=1-848 |
| 6W6E | EM | 3.7 Å | A/B/C/D/E/F=1-848 |
| 6DJU | EM | 3.8 Å | A/B/C/D/E/F=1-848 |
| 6DJV | EM | 3.9 Å | A/B/C/D/E/F=1-848 |
| 6ED3 | EM | 6.3 Å | A/B/C/D/E/F=1-848 |
| 7L6N | EM | 7.0 Å | A/B/C/D/E/F=1-848 |
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