Q9HD36: Bcl-2-like protein 10 (BCL2L10)

Bcl-2-like protein 10 (BCL2L10) is a 204-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9HD36.

Gene
BCL2L10
Organism
Homo sapiens
Length
204 residues
Mean pLDDT
85.1
Model
AF-Q9HD36-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.1 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate53%
70 to 90Confident: backbone generally right29%
50 to 70Low: treat with caution15%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

Promotes cell survival by suppressing apoptosis induced by BAX but not BAK (PubMed:11278245, PubMed:11689480). Increases binding of AHCYL1/IRBIT to ITPR1 (PubMed:27995898). Reduces ITPR1-mediated calcium release from the endoplasmic reticulum cooperatively with AHCYL1/IRBIT under normal cellular conditions (PubMed:27995898). Under apoptotic stress conditions, dissociates from ITPR1 and is displaced from mitochondria-associated endoplasmic reticulum membranes, leading to increased Ca(2+) transfer to mitochondria which promotes apoptosis (PubMed:27995898). Required for the correct formation of the microtubule organizing center during oocyte cell division, potentially via regulation of…

Subunit structure

Interacts with BAX (PubMed:11278245, PubMed:23235460). Interacts with BCL2 and BCL2L1/BCLX (PubMed:11278245, PubMed:11593390). Interacts with APAF1 (By similarity). Interacts with ITPR1, ITPR2 and ITPR3; the interaction with ITPR1 is increased in the presence of AHCLY1 (PubMed:27995898). Interacts with AHCYL1 (PubMed:27995898). Interacts with HIP1R (via ENTH and I/LWEQ domains)…

Subcellular location

Mitochondrion, Nucleus membrane, Endoplasmic reticulum, Cytoplasm, cytoskeleton, spindle

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4B4SX-ray1.9 ÅA=12-177

More AlphaFold highlights

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