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8B4W

X-ray structure of furin (PCSK3) in complex with 1H-isoindol-3-amine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VSILDDGIeknH
ChainResidueDetails
AVAL149-HIS160

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGTrCAGeVAA
ChainResidueDetails
AHIS194-ALA204

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSaSaPlAAG
ChainResidueDetails
AGLY366-GLY376

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues314
DetailsDomain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues132
DetailsDomain: {"description":"P/Homo B","evidences":[{"source":"PROSITE-ProRule","id":"PRU01173","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues21
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsMotif: {"description":"Cell attachment site","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24666235","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25974265","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4OMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RYD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24666235","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25974265","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4OMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RYD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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