Q9NZZ3: Charged multivesicular body protein 5 (CHMP5)

Charged multivesicular body protein 5 (CHMP5) is a 219-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NZZ3.

Gene
CHMP5
Organism
Homo sapiens
Length
219 residues
Mean pLDDT
79.4
Model
AF-Q9NZZ3-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.4 (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 accurate45%
70 to 90Confident: backbone generally right26%
50 to 70Low: treat with caution21%
Below 50Very low: often disordered regions9%

What pLDDT means and how to read it

Function

Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. 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. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is…

Subunit structure

Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. Interacts with VTA1; the interaction involves soluble CHMP5 (PubMed:15644320,…

Subcellular location

Cytoplasm, cytosol, Endosome membrane, Midbody

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4TXRX-ray1.0 ÅC=139-195
3UM2X-ray2.59 ÅB/E=200-219
3ULYX-ray2.6 ÅB=151-219
3UM1X-ray2.71 ÅB/E=151-219
3UM0X-ray3.1 ÅB=200-219
2LXMNMRB=139-195

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