O43521: Bcl-2-like protein 11 (BCL2L11)

Bcl-2-like protein 11 (BCL2L11) is a 198-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O43521.

Gene
BCL2L11
Organism
Homo sapiens
Length
198 residues
Mean pLDDT
60.1
Model
AF-O43521-F1 v6
Model created
1 Aug 2025
PDB structures
45

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Model confidence (pLDDT)

The mean pLDDT of this model is 60.1 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate7%
70 to 90Confident: backbone generally right20%
50 to 70Low: treat with caution35%
Below 50Very low: often disordered regions38%

What pLDDT means and how to read it

Function

Induces apoptosis and anoikis. Isoform BimL is more potent than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3 induce apoptosis, although less potent than isoform BimEL, isoform BimL and isoform BimS. Isoform Bim-gamma induces apoptosis. Isoform Bim-alpha3 induces apoptosis possibly through a caspase-mediated pathway. Isoform BimAC and isoform BimABC lack the ability to induce apoptosis

Subunit structure

Forms heterodimers with a number of antiapoptotic Bcl-2 proteins, including MCL1, BCL2, BCL2L1 isoform Bcl-X(L), BCL2A1/BFL-1, BHRF1, and BCL2L2/BCLW (PubMed:11997495, PubMed:18812174, PubMed:27013495). Does not heterodimerize with proapoptotic proteins such as BAD, BOK or BAK. Identified in a complex containing BCL2L11, DYNLL1 and BCL2L1 isoform Bcl-X(L); BH3 integrity is required for…

Subcellular location

Endomembrane system, Mitochondrion

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
6X8OX-ray1.31 ÅA/B/C/D=141-166
2WH6X-ray1.5 ÅB=141-166
4QVFX-ray1.53 ÅB=141-166
4A1UX-ray1.54 ÅB=146-163
2NL9X-ray1.55 ÅB=141-166
5VWYX-ray1.55 ÅB=141-166
6UA3X-ray1.55 ÅB=146-166
5VX0X-ray1.6 ÅB/D=141-166
5VWZX-ray1.62 ÅB/D=141-166
3KJ0X-ray1.7 ÅB=143-165
3FDLX-ray1.78 ÅB=141-166
2YQ6X-ray1.8 ÅB=147-164
4ZIEX-ray1.8 ÅC=141-166
5VX2X-ray1.85 ÅB/D=141-166
2YQ7X-ray1.9 ÅB=147-164
4B4SX-ray1.9 ÅB=141-166
5VWVX-ray1.9 ÅB=141-165
3KJ1X-ray1.94 ÅB=143-163
5VX3X-ray1.95 ÅB/D/F/H=141-166
6VBXX-ray1.95 ÅB=148-159

Showing 20 of 45 experimental structures (best resolution first).

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