Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5JXG

Structure of the unliganded form of the proprotein convertase furin.

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
AHOH751
AHOH786
AHOH1187

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
AHOH838
AHOH991
AHOH1110

site_idAC4
Number of Residues5
Detailsbinding site for residue NA A 604
ChainResidue
ATHR309
ASER311
ATHR314
ASER316
AHOH871

site_idAC5
Number of Residues8
Detailsbinding site for residue NA A 605
ChainResidue
AASP264
AGLY265
ANA606
ANA610
AHOH824
AHOH874
AHOH1175
AHOH1242

site_idAC6
Number of Residues7
Detailsbinding site for residue NA A 606
ChainResidue
ANA605
AHOH824
AHOH874
AHOH928
AHOH1242
AHOH1278
AHOH1304

site_idAC7
Number of Residues7
Detailsbinding site for residue NA A 607
ChainResidue
ASER279
AGLY284
AHOH733
AHOH765
AHOH1008
AHOH1213
AHOH1244

site_idAC8
Number of Residues4
Detailsbinding site for residue NA A 608
ChainResidue
ASER544
ASER544
AHOH823
AHOH823

site_idAC9
Number of Residues6
Detailsbinding site for residue NA A 609
ChainResidue
AGLU546
AGLU546
AHOH1063
AHOH1063
AHOH1177
AHOH1177

site_idAD1
Number of Residues6
Detailsbinding site for residue NA A 610
ChainResidue
AASP264
ANA605
AHOH850
AHOH1168
AHOH1175
AHOH1239

site_idAD2
Number of Residues6
Detailsbinding site for residue NA A 611
ChainResidue
ATHR413
AHOH840
AHOH907
AHOH947
AHOH1173
AHOH1289

site_idAD3
Number of Residues4
Detailsbinding site for residue CL A 612
ChainResidue
AARG276
ATYR313
ALYS449
ATYR571

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
AASN387
AASN440
AASN553

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon