P45880: Non-selective voltage-gated ion channel VDAC2 (VDAC2)

Non-selective voltage-gated ion channel VDAC2 (VDAC2) is a 294-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P45880.

Gene
VDAC2
Organism
Homo sapiens
Length
294 residues
Mean pLDDT
92.1
Model
AF-P45880-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 92.1 (very high 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 accurate82%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

Non-selective voltage-gated ion channel that mediates the transport of anions and cations through the mitochondrion outer membrane and plasma membrane (PubMed:8420959). The channel adopts an open conformation at zero mV and a closed conformation at both positive and negative potentials (PubMed:8420959). There are two populations of channels; the main that functions in a lower open-state conductance with lower ion selectivity, that switch, in a voltage-dependent manner, from the open to a low-conducting 'closed' state and the other that has a normal ion selectivity in the typical high conductance, 'open' state (PubMed:8420959). Binds various lipids, including the sphingolipid ceramide, the…

Subunit structure

Monomer, homodimer and higher order oligomers; formation of higher order structures is necessary for scramblase activity (PubMed:38065946). Interacts with ARMC12 in a TBC1D21-dependent manner (By similarity). Interacts with KLC3 (By similarity). Interacts with SPATA33 (By similarity). Interacts with PPP3CC in a SPATA33-dependent manner (By similarity). As a homodimer, interacts with the TOM…

Subcellular location

Mitochondrion outer membrane, Membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9EIIEM2.75 ÅF=1-294
9EIHEM3.1 ÅE/F=1-294
9EIJEM3.3 ÅE/F=1-294

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