P18708: Vesicle-fusing ATPase (NSF)

Vesicle-fusing ATPase (NSF) is a 744-residue protein from Cricetulus griseus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P18708.

Gene
NSF
Organism
Cricetulus griseus
Length
744 residues
Mean pLDDT
85.3
Model
AF-P18708-F1 v6
Model created
1 Aug 2025
PDB structures
42

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.3 (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 accurate42%
70 to 90Confident: backbone generally right48%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin. Interaction with AMPAR subunit GRIA2 leads to influence GRIA2 membrane cycling

Subunit structure

Homohexamer. Interacts with GABARAP and GABARAPL2 (By similarity). Interacts with GRIA2 (By similarity). Interacts with PLK2, leading to disrupt the interaction with GRIA2 (By similarity). Interacts with MUSK; may regulate MUSK endocytosis and activity (By similarity). Interacts with CDK16 (By similarity)

Subcellular location

Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1D2NX-ray1.75 ÅA=479-743
1NSFX-ray1.9 ÅA=478-744
1QCSX-ray1.9 ÅA=1-205
1QDNX-ray2.3 ÅA/B/C=1-203
9OJREM2.95 ÅA/B/C/D/E/F=1-744
9OJUEM2.97 ÅA/B/C/D/E/F=1-744
9PFFEM3.09 ÅA/B/C/D/E/F=1-744
9PFCEM3.15 ÅA/B/C/D/E/F=1-744
9OK5EM3.29 ÅA/B/C/D/E/F=1-744
9OJZEM3.39 ÅA/B/C/D/E/F=1-744
9PB9EM3.45 ÅA/B/C/D/E/F=1-744
9PBAEM3.47 ÅA/B/C/D/E/F=1-744
9OLJEM3.52 ÅA/B/C/D/E/F=1-744
9OLOEM3.56 ÅA/B/C/D/E/F=1-744
9PFGEM3.58 ÅJ/K=1-744
9NV9EM3.6 ÅA/B/C/D/E/F/G=1-744
9PAGEM3.62 ÅA/B/C/D/E/F=1-744
9PCZEM3.65 ÅA/B/C/D/E/F=1-744
9OKCEM3.67 ÅA/B/C/D/E/F=1-744
9PC3EM3.69 ÅA/B/C/D/E/F=1-744

Showing 20 of 42 experimental structures (best resolution first).

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