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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8EOK

Structure of the C3bB proconvertase in complex with lufaxin and factor Xa

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0035821biological_processmodulation of process of another organism
A0090729molecular_functiontoxin activity
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
D0004252molecular_functionserine-type endopeptidase activity
D0005576cellular_componentextracellular region
D0006508biological_processproteolysis
D0006956biological_processcomplement activation
G0004866molecular_functionendopeptidase inhibitor activity
H0004866molecular_functionendopeptidase inhibitor activity
H0005576cellular_componentextracellular region
H0005615cellular_componentextracellular space
L0005509molecular_functioncalcium ion binding
L0005576cellular_componentextracellular region
Functional Information from PROSITE/UniProt
site_idPS00477
Number of Residues9
DetailsALPHA_2_MACROGLOBULIN Alpha-2-macroglobulin family thiolester region signature. PsGCGEQnM
ChainResidueDetails
HPRO985-MET993
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
CLEU53-CYS58
DLEU497-CYS502
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDglgeYtCtC
ChainResidueDetails
LCYS61-CYS72
site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EcmEEtCsyeearEvfedsdktne.FW
ChainResidueDetails
LGLU16-TRP41
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CtCleGfeGKnC
ChainResidueDetails
LCYS70-CYS81
site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CtCleGFegkn....C
ChainResidueDetails
LCYS70-CYS81
LCYS109-CYS124
site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCetsp..........Cqnqgk..CkDglgeYtC
ChainResidueDetails
LASP46-CYS70
site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAcqGDSGGPHV
ChainResidueDetails
CASP189-VAL200
DASN668-ILE679
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17051150","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17684013","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2579379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues16
DetailsPeptide: {"description":"Complement C3f fragment","featureId":"PRO_0000005916","evidences":[{"source":"PubMed","id":"8376604","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues19
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues25
DetailsRegion: {"description":"Interaction with CFP/properdin","evidences":[{"source":"PubMed","id":"28264884","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31507604","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues3
DetailsSite: {"description":"Cleavage; by factor I","evidences":[{"source":"PubMed","id":"28671664","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Coordinates Mg(2+) for interaction with Complement factor B Bb fragment (CFB)","evidences":[{"source":"PubMed","id":"28264884","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31507604","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17051150","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsCross-link: {"description":"Isoglutamyl cysteine thioester (Cys-Gln)","evidences":[{"source":"PubMed","id":"1577777","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6175959","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues59
DetailsDomain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues57
DetailsDomain: {"description":"Sushi 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"10637221","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15016353","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q0P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsSite: {"description":"Cleavage; by CFD","evidences":[{"source":"PubMed","id":"6769474","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17310251","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6546754","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17310251","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19574954","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6546754","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"2006911","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17310251","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19503103","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19574954","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6546754","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WIN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22796577","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues232
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

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PDB entries from 2025-12-31

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