Q96S15: GATOR2 complex protein WDR24 (WDR24)

GATOR2 complex protein WDR24 (WDR24) is a 790-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96S15.

Gene
WDR24
Organism
Homo sapiens
Length
790 residues
Mean pLDDT
73.4
Model
AF-Q96S15-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 73.4 (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 accurate46%
70 to 90Confident: backbone generally right20%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions24%

What pLDDT means and how to read it

Function

Catalytic component of the GATOR2 complex, a multiprotein complex that acts as an activator of the amino acid-sensing branch of the mTORC1 signaling pathway (PubMed:23723238, PubMed:26449471, PubMed:26586190, PubMed:27487210, PubMed:35831510, PubMed:36528027, PubMed:36732624). The GATOR2 complex indirectly activates mTORC1 through the inhibition of the GATOR1 subcomplex (PubMed:23723238, PubMed:26449471, PubMed:26586190, PubMed:27487210, PubMed:35831510, PubMed:36528027, PubMed:36732624). GATOR2 probably acts as an E3 ubiquitin-protein ligase toward GATOR1 (PubMed:36528027, PubMed:36732624). In the presence of abundant amino acids, the GATOR2 complex mediates ubiquitination of the NPRL2…

Subunit structure

Component of the GATOR2 subcomplex, composed of MIOS, SEC13, SEH1L, WDR24 and WDR59 (PubMed:23723238, PubMed:35831510, PubMed:36528027). The GATOR2 complex interacts with CASTOR1 and CASTOR2; the interaction is negatively regulated by arginine (PubMed:26972053). The GATOR2 complex interacts with SESN1, SESN2 and SESN3; the interaction is negatively regulated by amino acids (PubMed:25263562,…

Subcellular location

Lysosome membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9LWFEM3.41 ÅC/I=1-790
9OTIEM3.5 ÅC/M=1-790
9LVKEM3.59 ÅC/M=1-790
7UHYEM3.66 ÅC=1-790
9LVJEM3.82 ÅC/M=1-790

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