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9IGO

PR3 S203A I221N W222N G223T mutant in complex with the extracellular domain of CD177

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005102molecular_functionsignaling receptor binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0006509biological_processmembrane protein ectodomain proteolysis
A0008236molecular_functionserine-type peptidase activity
A0008284biological_processpositive regulation of cell population proliferation
A0019730biological_processantimicrobial humoral response
A0019899molecular_functionenzyme binding
A0031012cellular_componentextracellular matrix
A0035578cellular_componentazurophil granule lumen
A0043547biological_processpositive regulation of GTPase activity
A0044853cellular_componentplasma membrane raft
A0045121cellular_componentmembrane raft
A0045217biological_processcell-cell junction maintenance
A0050765biological_processnegative regulation of phagocytosis
A0070062cellular_componentextracellular exosome
A0072672biological_processneutrophil extravasation
A0097029biological_processmature conventional dendritic cell differentiation
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU67-CYS72

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues220
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8757293","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FUJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

258009

PDB entries from 2026-08-12

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