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4TR2

Crystal structure of PvSUB1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0004252molecular_functionserine-type endopeptidase activity
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 801
ChainResidue
AASP281
AASP325
AVAL383
AASN386
AILE388
AILE390

site_idAC2
Number of Residues5
Detailsbinding site for residue CA A 802
ChainResidue
APRO135
AGLY190
AGLU129
AASN130
ATHR133

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 803
ChainResidue
AGLU336
AASP344
AASP346
AASN348
AVAL350
AASP353

site_idAC4
Number of Residues5
Detailsbinding site for residue CA A 804
ChainResidue
AGLU336
AARG340
AVAL343
AASP345
AASP352

site_idAC5
Number of Residues5
Detailsbinding site for residue PO4 A 805
ChainResidue
AASP438
AGLU439
ATYR440
AHIS484
ATYR486

site_idAC6
Number of Residues4
Detailsbinding site for residue PO4 A 806
ChainResidue
AASN303
AGLY384
AASN385
AHIS396

site_idAC7
Number of Residues4
Detailsbinding site for residue PO4 A 807
ChainResidue
AGLU129
AHIS131
ASER136
AGLU139

site_idAC8
Number of Residues6
Detailsbinding site for residue CA B 801
ChainResidue
BASP281
BASP325
BVAL383
BASN386
BILE388
BILE390

site_idAC9
Number of Residues5
Detailsbinding site for residue CA B 802
ChainResidue
BGLU129
BASN130
BTHR133
BPRO135
BGLY190

site_idAD1
Number of Residues6
Detailsbinding site for residue CA B 803
ChainResidue
BGLU336
BASP344
BASP346
BASN348
BVAL350
BASP353

site_idAD2
Number of Residues6
Detailsbinding site for residue CA B 804
ChainResidue
BGLU336
BARG340
BVAL343
BASP345
BASP352
BHOH903

site_idAD3
Number of Residues5
Detailsbinding site for residue PO4 B 805
ChainResidue
BASP438
BGLU439
BTYR440
BHIS484
BTYR486

site_idAD4
Number of Residues5
Detailsbinding site for residue PO4 B 806
ChainResidue
AARG452
BGLU129
BHIS131
BSER136
BGLU139

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. ICVIDSGIdynH
ChainResidueDetails
AILE312-HIS323

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVSGiISA
ChainResidueDetails
AHIS372-ALA382

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAA
ChainResidueDetails
AGLY547-ALA557

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues634
DetailsDomain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues22
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25204226","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4TR2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25204226","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37428845","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38503166","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4TR2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8COY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8COZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8QKE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8QKG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25204226","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37428845","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38503166","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4TR2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8COY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8COZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8QKG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Cleavage","evidences":[{"source":"PubMed","id":"37428845","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"37428845","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38503166","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8COY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8COZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8QKE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8QKG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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