Q15465: Sonic hedgehog protein (SHH)

Sonic hedgehog protein (SHH) is a 462-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15465.

Gene
SHH
Organism
Homo sapiens
Length
462 residues
Mean pLDDT
78.4
Model
AF-Q15465-F1 v6
Model created
1 Aug 2025
PDB structures
20

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 78.4 (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 accurate47%
70 to 90Confident: backbone generally right27%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions17%

What pLDDT means and how to read it

Function

Precursor of sonic hedgehog, a morphogen that activates the smoothened signaling pathway, and which is essential for a variety of patterning events during development (PubMed:29954986, PubMed:29995851, PubMed:30139912, PubMed:31127104, PubMed:31548691). The C-terminal part of the precursor displays an autoproteolysis and a cholesterol transferase activity, resulting (1) in the cleavage of the full-length protein into two parts, Sonic hedgehog protein N-product and C-product (ShhN and ShhC, respectively) and (2) covalent attachment of a cholesterol moiety to the C-terminus of the newly generated ShhN (By similarity). Both autoproteolysis and a cholesterol transferase activities occur in the…

Subunit structure

Interacts with HHATL/GUP1 which negatively regulates HHAT-mediated palmitoylation of the SHH N-terminus (By similarity). Interacts with HHIP (PubMed:19561609). Interacts with glypican GPC3 (By similarity)

Subcellular location

Endoplasmic reticulum membrane, Golgi apparatus membrane, Secreted, Cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6PJVX-ray1.43 ÅA=29-197
8Z3AX-ray1.75 ÅA=29-197
8Z39X-ray1.8 ÅA=29-197
3MXWX-ray1.83 ÅA=29-197
3M1NX-ray1.85 ÅA/B=23-197
8Z2VX-ray1.89 ÅA=29-197
8YYZX-ray1.9 ÅA=29-197
7URFEM2.8 ÅB=24-30
3HO5X-ray3.01 ÅH=29-197
7MHZEM3.2 ÅB=24-31
6RMGEM3.4 ÅB=21-197
6E1HEM3.5 ÅC=24-197
6RVDEM3.5 ÅC=24-197
7RHQEM3.53 ÅC=24-197
6DMYEM3.6 ÅB=24-197
6N7HEM3.6 ÅC=24-197
6OEVEM3.8 ÅC=23-197
7E2IEM4.07 ÅG=1-462
6N7KEM6.5 ÅC/F=24-197
6N7GEM6.8 ÅC/F=24-197

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.