Alpha-crystallin B chain (CRYAB) is a 175-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P02511.
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The mean pLDDT of this model is 75.8 (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 | 40% |
| 70 to 90 | Confident: backbone generally right | 22% |
| 50 to 70 | Low: treat with caution | 22% |
| Below 50 | Very low: often disordered regions | 17% |
What pLDDT means and how to read it
May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity)
Heteromer composed of three CRYAA and one CRYAB subunits (PubMed:20836128). Aggregates with homologous proteins, including the small heat shock protein HSPB1, to form large heteromeric complexes (PubMed:10751411). Inter-subunit bridging via zinc ions enhances stability, which is crucial as there is no protein turn over in the lens (PubMed:22890888). Interacts with HSPBAP1 and TTN/titin…
Cytoplasm, Nucleus, Secreted, Lysosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4M5S | X-ray | 1.37 Å | A=68-153, B=156-164 |
| 3SGP | X-ray | 1.4 Å | A/B/C/D=90-100 |
| 7ROJ | X-ray | 1.6 Å | A/B/C/D/E/F/G/H/I/J/K/L=90-100 |
| 3SGM | X-ray | 1.7 Å | A/B/C/D=90-100 |
| 3SGS | X-ray | 1.7 Å | A=95-100 |
| 2Y1Y | X-ray | 2.0 Å | A=71-157 |
| 4M5T | X-ray | 2.0 Å | A/C/E/G=68-153, B/D/F/H=156-164 |
| 3SGR | X-ray | 2.17 Å | A/B/C/D/E/F=90-100 |
| 2Y1Z | X-ray | 2.5 Å | A/B=67-157 |
| 3SGO | X-ray | 2.56 Å | A=90-100 |
| 2WJ7 | X-ray | 2.63 Å | A/B/C/D/E=64-157 |
| 5VVV | X-ray | 2.8 Å | B/D=38-50 |
| 3SGN | X-ray | 2.81 Å | A/B=90-100 |
| 3L1G | X-ray | 3.32 Å | A=68-162 |
| 9BEE | EM | 3.4 Å | B=76-163 |
| 2Y22 | X-ray | 3.7 Å | A/B/C/D/E/F=67-157 |
| 2YGD | EM | 9.4 Å | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-175 |
| 2KLR | NMR | A/B=1-175 | |
| 2N0K | NMR | A/B=64-152 | |
| 3J07 | Other | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-175 |
Showing 20 of 21 experimental structures (best resolution first).
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