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5JXH

Structure the proprotein convertase furin in complex with meta-guanidinomethyl-Phac-RVR-Amba at 2.0 Angstrom resolution.

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
AHOH780
AHOH859
AHOH1131

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
AHOH815
AHOH856
AHOH973

site_idAC4
Number of Residues4
Detailsbinding site for residue NA A 604
ChainResidue
ATHR309
ASER311
ATHR314
AHOH830

site_idAC5
Number of Residues6
Detailsbinding site for residue NA A 605
ChainResidue
ASER279
AGLY284
AHOH726
AHOH848
AHOH1135
AHOH1155

site_idAC6
Number of Residues4
Detailsbinding site for residue NA A 606
ChainResidue
ASER544
ASER544
AHOH781
AHOH781

site_idAC7
Number of Residues6
Detailsbinding site for residue NA A 607
ChainResidue
AASP264
AHOH898
AHOH907
AHOH1012
AHOH1138
AHOH1210

site_idAC8
Number of Residues4
Detailsbinding site for residue CL A 608
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

217705

數據於2024-03-27公開中

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