Q15388: Mitochondrial import receptor subunit TOM20 homolog (TOMM20)

Mitochondrial import receptor subunit TOM20 homolog (TOMM20) is a 145-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15388.

Gene
TOMM20
Organism
Homo sapiens
Length
145 residues
Mean pLDDT
76.4
Model
AF-Q15388-F1 v6
Model created
1 Aug 2025
PDB structures
12

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Model confidence (pLDDT)

The mean pLDDT of this model is 76.4 (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 accurate11%
70 to 90Confident: backbone generally right61%
50 to 70Low: treat with caution25%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

Central receptor component of the translocase of the outer membrane of mitochondria (TOM) complex essential for the recognition and translocation of cytosolically synthesized mitochondrial preproteins (PubMed:40080546). Together with TOMM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore (PubMed:18331822). The TOM complex associates with the ion channel VDAC2 and PINK1 kinase at depolarized mitochondria, this interaction stabilizes PINK1 at the outer mitochondrial membrane and triggers downstream mitophagy by the recruitment of the E3 ubiquitin ligase PRKN…

Subunit structure

Part of the translocase of the outer mitochondrial membrane (TOM complex) consisting of at least TOMM5, TOMM6, TOMM7, TOMM20, TOMM22 and TOMM40 (PubMed:18331822, PubMed:40080546). TOMM70 may also be found in the TOM complex (PubMed:18331822). The TOM complex interacts with the VDAC2 homodimer (PubMed:40080546). Upon mitochondrial depolarization, the TOM-VDAC assembly interacts with PINK1; the…

Subcellular location

Mitochondrion outer membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4APOX-ray1.9 ÅD/E=140-145
7VBYEM2.54 ÅB/I=1-145
9EIIEM2.75 ÅD=1-145
9EIHEM3.1 ÅC/D=1-145
8UY3X-ray3.2 ÅJ/K/M=62-127
9EIJEM3.3 ÅD=1-145
9JCEEM3.59 ÅB=25-145
9J79EM4.08 ÅB/C/G/S=25-145
9J7BEM4.12 ÅB/C/G/Q/S=25-145
9J7AEM4.13 ÅB/C=25-145
8XVAEM5.92 ÅK=1-145
7VC9EM13.0 ÅM/N=1-145

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