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8SNO

Structure of mature human ADAM17/iRhom2 sheddase complex, conformation 2

Functional Information from GO Data
ChainGOidnamespacecontents
B0002862biological_processnegative regulation of inflammatory response to antigenic stimulus
B0004252molecular_functionserine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005796cellular_componentGolgi lumen
B0005886cellular_componentplasma membrane
B0015031biological_processprotein transport
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 Residues435
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
BMET1-LEU409
BPHE682-ALA692
BPRO737-GLY747
BTYR795-PRO802

site_idSWS_FT_FI2
Number of Residues140
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BVAL410-VAL430
BTRP661-ILE681
BGLY693-LEU713
BPRO716-LEU736
BPHE748-ASP768
BALA774-LEU794
BTRP803-ASP823

site_idSWS_FT_FI3
Number of Residues234
DetailsTOPO_DOM: Lumenal => ECO:0000255
ChainResidueDetails
BGLY431-GLY660
BGLU714-ARG715
BLYS769-ARG773

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
BARG90
BALA325
BVAL328

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BARG113
AHIS409
AHIS415

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q80WQ6
ChainResidueDetails
BHIS117
BARG323

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR761

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Z1K9
ChainResidueDetails
ASER767

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
ASER791

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:12621058
ChainResidueDetails
ASER819

site_idSWS_FT_FI11
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN264
AASN452
AASN498
AASN539
AASN551
AASN594

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PDB entries from 2024-07-17

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