P78536: Disintegrin and metalloproteinase domain-containing protein 17 (ADAM17)

Disintegrin and metalloproteinase domain-containing protein 17 (ADAM17) is a 824-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P78536.

Gene
ADAM17
Organism
Homo sapiens
Length
824 residues
Mean pLDDT
72.7
Model
AF-P78536-F1 v6
Model created
1 Aug 2025
PDB structures
31

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Model confidence (pLDDT)

The mean pLDDT of this model is 72.7 (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 accurate25%
70 to 90Confident: backbone generally right42%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions23%

What pLDDT means and how to read it

Function

Transmembrane metalloprotease which mediates the ectodomain shedding of a myriad of transmembrane proteins including adhesion proteins, growth factor precursors and cytokines important for inflammation and immunity (PubMed:24226769, PubMed:24227843, PubMed:28060820, PubMed:28923481, PubMed:38771644). Cleaves the membrane-bound precursor of TNF to its mature soluble form (PubMed:36078095, PubMed:9034191). Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (PubMed:20592283). Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth…

Subunit structure

Interacts with MAD2L1, MAPK14 and MUC1 (PubMed:12441351, PubMed:20188673). Interacts with iRhom1/RHBDF1 and iRhom2/RHBDF2 (PubMed:29897333). Interacts with FRMD8 via its interaction with iRhom1/RHBDF1 and iRhom2/RHBDF2 (PubMed:29897333). Interacts with TSPAN8 (PubMed:36078095)

Subcellular location

Cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2DDFX-ray1.7 ÅA/B=218-474
8CQYX-ray1.7 ÅB=813-824
3L0VX-ray1.75 ÅA/B=215-476
3EWJX-ray1.8 ÅA/B=215-477
3KMCX-ray1.8 ÅA/B=215-476
3KMEX-ray1.85 ÅA/B=215-476
3LE9X-ray1.85 ÅA/B=215-476
3O64X-ray1.88 ÅA/B=215-476
2I47X-ray1.9 ÅA/B/C/D=212-493
3E8RX-ray1.9 ÅA/B=215-477
3EDZX-ray1.9 ÅA/B=215-477
3LGPX-ray1.9 ÅA/B=215-476
3L0TX-ray1.92 ÅA/B=215-476
1BKCX-ray2.0 ÅA/C/E/I=219-474
2OI0X-ray2.0 ÅA=216-477
3B92X-ray2.0 ÅA=216-474
3LEAX-ray2.0 ÅA/B=215-476
2FV9X-ray2.02 ÅA/B=218-475
2FV5X-ray2.1 ÅA/B=216-475
3G42X-ray2.1 ÅA/B/C/D=212-492

Showing 20 of 31 experimental structures (best resolution first).

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