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5MIM

Xray structure of human furin bound with the 2,5-dideoxystreptamine derived small molecule inhibitor 1n

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 601
ChainResidue
AASP174
AASP179
AASP181
AHOH736
AHOH762
AHOH1071

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 602
ChainResidue
AASN208
AVAL210
AGLY212
AASP115
AASP162
AVAL205

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 603
ChainResidue
AASP258
AASP301
AGLU331
AHOH825
AHOH932
AHOH1023

site_idAC4
Number of Residues5
Detailsbinding site for residue NA A 604
ChainResidue
ATHR309
ASER311
ATHR314
ASER316
AHOH867

site_idAC5
Number of Residues6
Detailsbinding site for residue NA A 605
ChainResidue
ASER279
AGLY284
AHOH748
AHOH757
AHOH1104
AHOH1121

site_idAC6
Number of Residues4
Detailsbinding site for residue NA A 606
ChainResidue
ASER544
ASER544
AHOH804
AHOH804

site_idAC7
Number of Residues6
Detailsbinding site for residue NA A 607
ChainResidue
AGLU546
AGLU546
AHOH1074
AHOH1074
AHOH1089
AHOH1089

site_idAC8
Number of Residues4
Detailsbinding site for residue CL A 608
ChainResidue
AARG276
ATYR313
ALYS449
ATYR571

site_idAC9
Number of Residues7
Detailsbinding site for residue 1N A 609
ChainResidue
AARG185
AASP191
AASN192
ALEU227
AASP228
AGLY229
AGLU230

site_idAD1
Number of Residues13
Detailsbinding site for residue 1N A 610
ChainResidue
AASP153
AHIS194
ACYS198
ALEU227
AVAL231
AGLU236
ASER253
AGLY255
AASP264
ATYR308
ASER368
AHOH770
AHOH1025

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

246031

PDB entries from 2025-12-10

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