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8SNL

Structure of human ADAM17/iRhom2 sheddase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
B0002862biological_processnegative regulation of inflammatory response to antigenic stimulus
B0004252molecular_functionserine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005796cellular_componentGolgi lumen
B0005886cellular_componentplasma membrane
B0012505cellular_componentendomembrane system
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0019838molecular_functiongrowth factor binding
B0042058biological_processregulation of epidermal growth factor receptor signaling pathway
B0050708biological_processregulation of protein secretion
B0050709biological_processnegative regulation of protein secretion
B0072659biological_processprotein localization to plasma membrane
B0140318molecular_functionprotein transporter activity
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VTTHELGHNF
ChainResidueDetails
AVAL402-PHE411

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues160
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues251
DetailsDomain: {"description":"Peptidase M12B","evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues88
DetailsDomain: {"description":"Disintegrin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00068","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues68
DetailsRegion: {"description":"Crambin-like"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues7
DetailsMotif: {"description":"Cysteine switch","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9520379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"description":"in inhibited form","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9520379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues9
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues266
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues27
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues22
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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