P58004: Sestrin-2 (SESN2)

Sestrin-2 (SESN2) is a 480-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P58004.

Gene
SESN2
Organism
Homo sapiens
Length
480 residues
Mean pLDDT
81.4
Model
AF-P58004-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.4 (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 accurate66%
70 to 90Confident: backbone generally right10%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions17%

What pLDDT means and how to read it

Function

Functions as an intracellular leucine sensor that negatively regulates the mTORC1 signaling pathway through the GATOR complex (PubMed:18692468, PubMed:25263562, PubMed:25457612, PubMed:26449471, PubMed:26586190, PubMed:26612684, PubMed:31586034, PubMed:35114100, PubMed:35831510, PubMed:36528027). In absence of leucine, binds the GATOR subcomplex GATOR2 and prevents mTORC1 signaling (PubMed:18692468, PubMed:25263562, PubMed:25457612, PubMed:26449471, PubMed:26586190, PubMed:26612684, PubMed:31586034, PubMed:35114100, PubMed:35831510, PubMed:36528027). Binding of leucine to SESN2 disrupts its interaction with GATOR2 thereby activating the TORC1 signaling pathway (PubMed:26449471,…

Subunit structure

Interacts with the GATOR2 complex which is composed of MIOS, SEC13, SEH1L, WDR24 and WDR59; the interaction is negatively regulated by leucine (PubMed:25263562, PubMed:25457612, PubMed:26449471, PubMed:35114100, PubMed:35831510, PubMed:36528027). Conveys leucine availability via direct interaction with SEH1L and WDR24 components of the GATOR2 complex (PubMed:35831510, PubMed:36528027). Interacts…

Subcellular location

Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5DJ4X-ray2.7 ÅA/B/C/D/E=1-480
5T0NX-ray3.0 ÅA/B/C/D/E=1-480
6N0MX-ray3.3 ÅA/B/C/D/E=66-480
9LWFEM3.41 ÅX/Y=1-480
5CUFX-ray3.5 ÅA/B/C/D/E=1-480
9LVJEM3.82 ÅU/V=1-480

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