P30874: Somatostatin receptor type 2 (SSTR2)

Somatostatin receptor type 2 (SSTR2) is a 369-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P30874.

Gene
SSTR2
Organism
Homo sapiens
Length
369 residues
Mean pLDDT
81.3
Model
AF-P30874-F1 v6
Model created
1 Aug 2025
PDB structures
17

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.3 (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 accurate54%
70 to 90Confident: backbone generally right24%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions12%

What pLDDT means and how to read it

Function

Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and PLC via pertussis toxin insensitive as well as sensitive G proteins. Inhibits calcium entry by suppressing voltage-dependent calcium channels. Acts as the functionally dominant somatostatin receptor in pancreatic alpha- and beta-cells where it mediates the inhibitory effect of somatostatin-14 on hormone secretion. Inhibits cell growth through enhancement of MAPK1 and MAPK2 phosphorylation and subsequent up-regulation of CDKN1B. Stimulates neuronal migration and axon outgrowth and may participate…

Subunit structure

Homodimer and heterodimer with SSTR3 and SSTR5. Heterodimerization with SSTR3 inactivates SSTR3 receptor function. Heterodimerization with SSTR5 is enhanced by agonist stimulation of SSTR2 and increases SSTR2 cell growth inhibition activity. Following agonist stimulation, homodimers dissociate into monomers which is required for receptor internalization. Interacts with beta-arrestin; this…

Subcellular location

Cell membrane, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7T10EM2.5 ÅR=1-237, R=253-369
7XN9X-ray2.6 ÅA=2-239, A=243-359
7XNAX-ray2.65 ÅA=2-237, A=244-359
7T11EM2.7 ÅR=1-237, R=253-369
7WIGEM2.7 ÅR=1-369
7WICEM2.8 ÅR=1-369
7XATEM2.85 ÅA=1-361
7XAVEM2.87 ÅA=1-361
7XAUEM2.97 ÅA=1-361
7UL5EM3.1 ÅA=1-237, A=254-369
7XMREM3.1 ÅR=2-359
7YACEM3.24 ÅE=31-338
7Y24EM3.25 ÅE=1-327
7Y26EM3.3 ÅE=1-337
7YAEEM3.37 ÅE=1-369
7Y27EM3.48 ÅE=1-337
7WJ5EM3.72 ÅR=1-369

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