Q9NP79: Vacuolar protein sorting-associated protein VTA1 homolog (VTA1)

Vacuolar protein sorting-associated protein VTA1 homolog (VTA1) is a 307-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NP79.

Gene
VTA1
Organism
Homo sapiens
Length
307 residues
Mean pLDDT
78.3
Model
AF-Q9NP79-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 78.3 (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 accurate63%
70 to 90Confident: backbone generally right4%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions28%

What pLDDT means and how to read it

Function

Involved in the endosomal multivesicular bodies (MVB) pathway. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. Thought to be a cofactor of VPS4A/B, which catalyzes disassembles membrane-associated ESCRT-III assemblies. Involved in the sorting and down-regulation of EGFR (By similarity). Involved in HIV-1 budding

Subunit structure

Interacts with VPS4B. Interacts with CHMP1B. Interacts with CHMP2A; the interaction probably involves the open conformation of (polymerized) CHMP2A. Interacts with CHMP3. Interacts with CHMP5; the interaction involves soluble CHMP5. Interacts with IST1

Subcellular location

Cytoplasm, Endosome membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4TXRX-ray1.0 ÅA=1-162
4U7EX-ray1.6 ÅB=1-162
4TXQX-ray2.21 ÅA/B=1-162
4TXPX-ray3.01 ÅA/B/C=1-162
2LXLNMRA=1-183
2LXMNMRA=1-168

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