Q9VKJ9: Coiled-coil and C2 domain-containing protein 1-like (l(2)gd1)

Coiled-coil and C2 domain-containing protein 1-like (l(2)gd1) is a 816-residue protein from Drosophila melanogaster. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9VKJ9.

Gene
l(2)gd1
Organism
Drosophila melanogaster
Length
816 residues
Mean pLDDT
74.0
Model
AF-Q9VKJ9-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 74.0 (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 accurate35%
70 to 90Confident: backbone generally right28%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions24%

What pLDDT means and how to read it

Function

Phosphatidyl inositol monophosphate binding protein involved in endosomal protein sorting through regulation of the endosomal sorting required for transport (ESCRT) pathway (PubMed:17084357, PubMed:28564595, PubMed:33349255). Required for full activity of the ESCRT-III complex core component shrb/shrub, probably by preventing its inappropriate polymerization (PubMed:28564595, PubMed:33349255). Required, but not essential, for the efficient generation of intraluminal vesicles (ILVs) in multivesicular bodies (MVBs) (PubMed:33349255). Involved in a late stage of the endosomal pathway targeting transmembrane proteins of the plasma membrane for lysosomal degradation (PubMed:17084357,…

Subunit structure

Interacts (via DM14 domains 1 and 3) with shrb; the interaction is direct and blocks access to the surface involved in shrb polymerization (PubMed:22389409, PubMed:27452459, PubMed:28564595). This interaction may be required for the ESCRT-III complex role in multivesicular body formation (PubMed:22389409)

Subcellular location

Cytoplasm, Cytoplasm, cytosol, Apicolateral cell membrane, Cytoplasm, cell cortex, Endosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5VNYX-ray1.1 ÅA=359-423
5VO5X-ray2.0 ÅA=359-423
6EI6X-ray2.46 ÅA/B=550-816
7ZSSEM2.63 ÅD/P/h=359-423
7ZRVEM2.8 ÅE/F=356-423
7ZSDEM3.29 ÅP=359-423

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