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4Z2A

Crystal structure of unglycosylated apo human furin @1.89A

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
AASP115
AASP162
AVAL205
AASN208
AVAL210
AGLY212

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 602
ChainResidue
AHOH745
AHOH864
AHOH1047
AASP174
AASP179
AASP181

site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 603
ChainResidue
ATHR309
ASER311
ATHR314
ASER316
AHOH788

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 604
ChainResidue
AASP258
AASP301
AGLU331
AHOH777
AHOH925
AHOH1001

site_idAC5
Number of Residues7
Detailsbinding site for residue PO4 A 605
ChainResidue
AARG193
AHIS194
AARG197
ASER363
AHIS364
ATHR365
APO4606

site_idAC6
Number of Residues6
Detailsbinding site for residue PO4 A 606
ChainResidue
AARG193
AARG197
AHIS300
ASER363
AHIS521
APO4605

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO A 607
ChainResidue
AARG298
ATRP328
ATHR365
AGLY366
AHOH950

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 Residues3
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
ChainResidueDetails
AASP153
AHIS194
ASER368

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
ChainResidueDetails
AASP115
AASP258
AASP301
AGLU331
AASP162
AASP174
AASP179
AASP181
AVAL205
AASN208
AVAL210
AGLY212

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
ChainResidueDetails
AASP154
AASP191
AGLU236
ASER253
AASP264
AALA292
AASP306
ATYR308
ASER368

site_idSWS_FT_FI4
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASP387
AASP440
AASN553

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PDB entries from 2024-05-01

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