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8SNM

Structure of mature human ADAM17/iRhom2 sheddase complex in complex with ADAM17 prodomain

Functional Information from GO Data
ChainGOidnamespacecontents
C0002862biological_processnegative regulation of inflammatory response to antigenic stimulus
C0004252molecular_functionserine-type endopeptidase activity
C0005515molecular_functionprotein binding
C0005783cellular_componentendoplasmic reticulum
C0005789cellular_componentendoplasmic reticulum membrane
C0005796cellular_componentGolgi lumen
C0005886cellular_componentplasma membrane
C0015031biological_processprotein transport
C0019838molecular_functiongrowth factor binding
C0042058biological_processregulation of epidermal growth factor receptor signaling pathway
C0050708biological_processregulation of protein secretion
C0050709biological_processnegative regulation of protein secretion
C0072659biological_processprotein localization to plasma membrane
C0140318molecular_functionprotein transporter activity
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VTTHELGHNF
ChainResidueDetails
BVAL402-PHE411

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues456
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
BARG215-ASN671
CPHE682-ALA692
CPRO737-GLY747
CTYR795-PRO802

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BILE672-HIS692
AASN157
AASN174
CPRO716-LEU736
CPHE748-ASP768
CALA774-LEU794
CTRP803-ASP823

site_idSWS_FT_FI3
Number of Residues131
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
BCYS693-CYS824
CGLU714-ARG715
CLYS769-ARG773

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:9520379
ChainResidueDetails
BGLU406
CALA325
CVAL328

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:9520379
ChainResidueDetails
BHIS405
BHIS409
BHIS415

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:12058067, ECO:0000269|PubMed:20188673
ChainResidueDetails
BTHR735
CARG323

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BTHR761

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Z1K9
ChainResidueDetails
BSER767

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER791

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:12621058
ChainResidueDetails
BSER819

site_idSWS_FT_FI11
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN264
BASN452
BASN498
BASN539
BASN551
BASN594

223790

PDB entries from 2024-08-14

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