O75351: Vacuolar protein sorting-associated protein 4B (VPS4B)

Vacuolar protein sorting-associated protein 4B (VPS4B) is a 444-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O75351.

Gene
VPS4B
Organism
Homo sapiens
Length
444 residues
Mean pLDDT
85.9
Model
AF-O75351-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.9 (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 accurate65%
70 to 90Confident: backbone generally right21%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions7%

What pLDDT means and how to read it

Function

Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their ATP-dependent disassembly, possibly in combination with membrane fission (PubMed:18687924). Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. 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. VPS4A/B are required for the exosomal release of SDCBP, CD63 and syndecan…

Subunit structure

Proposed to be monomeric or homodimeric in nucleotide-free form and to oligomerize upon binding to ATP to form two stacked hexameric or heptameric rings with a central pore through which ESCRT-III substrates are translocated in an ATP-dependent manner. In vitro, associates on the inside of a helical tubular structure formed by a CHMP2A-CHMP3 polymer. Interacts with CHMP1A, CHMP1B, CHMP2A, CHMP4B…

Subcellular location

Late endosome membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4U7YX-ray2.5 ÅA=1-89
1XWIX-ray2.8 ÅA=123-444
7L9XX-ray2.81 ÅA=1-444
1WR0NMRA=1-77
2CPTNMRA=1-104
2JQHNMRA=1-86
2JQKNMRA=1-86

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