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4LVO

Crystal structure of PfSUB1-prodomain-NIMP.M7 Fab complex with added CaCl2

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 701
ChainResidue
AGLU338
AASP381
AILE439
AASN442
AILE444
AVAL446

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 702
ChainResidue
AASP401
AASP408
CHOH327
AGLU392
AARG396
APHE399

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 703
ChainResidue
AGLU392
AASP400
AASP402
AASN404
AILE406
AASP409

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. ICVIDSGIdynH
ChainResidueDetails
AILE368-HIS379

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVSGiISA
ChainResidueDetails
AHIS428-ALA438

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAaPhVAA
ChainResidueDetails
AGLY604-ALA614

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
BTYR193-HIS199

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues318
DetailsDomain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24785947","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LVO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q8I0V0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Cleavage; by PMX","evidences":[{"source":"UniProtKB","id":"Q8I0V0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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