E3 ubiquitin-protein ligase CBL-B (CBLB) is a 982-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13191.
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The mean pLDDT of this model is 61.9 (low 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 | 28% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 52% |
What pLDDT means and how to read it
E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome (PubMed:20525694, PubMed:40101708). Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways (PubMed:40101708). In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production (By similarity). Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation (PubMed:11087752,…
Interacts with SH3 domain-containing proteins LCK, CRK and SORBS1. Interacts with LCP2 and ZAP70. Interacts with CBL (PubMed:29237719). Interacts with SH3 domain-containing proteins VAV1, FYN, FGR, PLCG1, GRB2, CRKL, PIK3R1 and SH3KBP1/CIN85. Identified in heterotrimeric complexes with SH3KBP1/CIN85, CD2AP and ARHGEF7, where one CBLB peptide binds two copies of the other protein. Interacts with…
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8QTG | X-ray | 1.42 Å | A=36-427 |
| 8QTJ | X-ray | 1.52 Å | A=36-427 |
| 2OOA | X-ray | 1.56 Å | A/B=924-973 |
| 9FQJ | X-ray | 1.56 Å | A/B=36-427 |
| 2J6F | X-ray | 1.7 Å | C=902-912 |
| 8VW5 | X-ray | 1.76 Å | A/B=36-343 |
| 9FQH | X-ray | 1.79 Å | A=36-427 |
| 8GCY | X-ray | 1.81 Å | A=38-427 |
| 2AK5 | X-ray | 1.85 Å | D=904-911 |
| 8QTK | X-ray | 1.87 Å | A=36-427 |
| 2OOB | X-ray | 1.9 Å | A=924-973 |
| 9FQI | X-ray | 1.95 Å | A=36-427 |
| 2BZ8 | X-ray | 2.0 Å | C=902-912 |
| 8QNH | X-ray | 2.0 Å | A=36-427 |
| 8QNG | X-ray | 2.2 Å | A=36-427 |
| 8QTH | X-ray | 2.2 Å | A=36-427 |
| 3ZNI | X-ray | 2.21 Å | A/E/I/M=36-427 |
| 3PFV | X-ray | 2.27 Å | A/B=38-344 |
| 8VW4 | X-ray | 2.4 Å | A/B=36-343 |
| 8QNI | X-ray | 2.48 Å | A=36-427 |
Showing 20 of 24 experimental structures (best resolution first).
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