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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2XWJ

Crystal Structure of Complement C3b in Complex with Factor B

Functional Information from GO Data
ChainGOidnamespacecontents
A0004866molecular_functionendopeptidase inhibitor activity
B0004866molecular_functionendopeptidase inhibitor activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
C0004866molecular_functionendopeptidase inhibitor activity
D0004866molecular_functionendopeptidase inhibitor activity
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
E0004866molecular_functionendopeptidase inhibitor activity
F0004866molecular_functionendopeptidase inhibitor activity
F0005576cellular_componentextracellular region
F0005615cellular_componentextracellular space
G0004866molecular_functionendopeptidase inhibitor activity
H0004866molecular_functionendopeptidase inhibitor activity
H0005576cellular_componentextracellular region
H0005615cellular_componentextracellular space
I0001848molecular_functioncomplement binding
I0002376biological_processimmune system process
I0004252molecular_functionserine-type endopeptidase activity
I0005515molecular_functionprotein binding
I0005576cellular_componentextracellular region
I0005615cellular_componentextracellular space
I0005886cellular_componentplasma membrane
I0006508biological_processproteolysis
I0006956biological_processcomplement activation
I0006957biological_processcomplement activation, alternative pathway
I0008233molecular_functionpeptidase activity
I0008236molecular_functionserine-type peptidase activity
I0009617biological_processresponse to bacterium
I0009986cellular_componentcell surface
I0016787molecular_functionhydrolase activity
I0045087biological_processinnate immune response
I0070062cellular_componentextracellular exosome
I0072562cellular_componentblood microparticle
I0106139cellular_componentsymbiont cell surface
J0001848molecular_functioncomplement binding
J0002376biological_processimmune system process
J0004252molecular_functionserine-type endopeptidase activity
J0005515molecular_functionprotein binding
J0005576cellular_componentextracellular region
J0005615cellular_componentextracellular space
J0005886cellular_componentplasma membrane
J0006508biological_processproteolysis
J0006956biological_processcomplement activation
J0006957biological_processcomplement activation, alternative pathway
J0008233molecular_functionpeptidase activity
J0008236molecular_functionserine-type peptidase activity
J0009617biological_processresponse to bacterium
J0009986cellular_componentcell surface
J0016787molecular_functionhydrolase activity
J0045087biological_processinnate immune response
J0070062cellular_componentextracellular exosome
J0072562cellular_componentblood microparticle
J0106139cellular_componentsymbiont cell surface
K0001848molecular_functioncomplement binding
K0002376biological_processimmune system process
K0004252molecular_functionserine-type endopeptidase activity
K0005515molecular_functionprotein binding
K0005576cellular_componentextracellular region
K0005615cellular_componentextracellular space
K0005886cellular_componentplasma membrane
K0006508biological_processproteolysis
K0006956biological_processcomplement activation
K0006957biological_processcomplement activation, alternative pathway
K0008233molecular_functionpeptidase activity
K0008236molecular_functionserine-type peptidase activity
K0009617biological_processresponse to bacterium
K0009986cellular_componentcell surface
K0016787molecular_functionhydrolase activity
K0045087biological_processinnate immune response
K0070062cellular_componentextracellular exosome
K0072562cellular_componentblood microparticle
K0106139cellular_componentsymbiont cell surface
L0001848molecular_functioncomplement binding
L0002376biological_processimmune system process
L0004252molecular_functionserine-type endopeptidase activity
L0005515molecular_functionprotein binding
L0005576cellular_componentextracellular region
L0005615cellular_componentextracellular space
L0005886cellular_componentplasma membrane
L0006508biological_processproteolysis
L0006956biological_processcomplement activation
L0006957biological_processcomplement activation, alternative pathway
L0008233molecular_functionpeptidase activity
L0008236molecular_functionserine-type peptidase activity
L0009617biological_processresponse to bacterium
L0009986cellular_componentcell surface
L0016787molecular_functionhydrolase activity
L0045087biological_processinnate immune response
L0070062cellular_componentextracellular exosome
L0072562cellular_componentblood microparticle
L0106139cellular_componentsymbiont cell surface
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ILEU497-CYS502
site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. NTcrGDSGGPLI
ChainResidueDetails
IASN668-ILE679
site_idPS00477
Number of Residues9
DetailsALPHA_2_MACROGLOBULIN Alpha-2-macroglobulin family thiolester region signature. PsGCGEEnM
ChainResidueDetails
BPRO985-MET993
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSite: {"description":"(Microbial infection) Cleavage; by S.pyogenes SpeB","evidences":[{"source":"PubMed","id":"18160402","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues28
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
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_FI4
Number of Residues64
DetailsPeptide: {"description":"Complement C3f fragment","featureId":"PRO_0000005916","evidences":[{"source":"PubMed","id":"8376604","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues76
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues100
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_FI7
Number of Residues12
DetailsSite: {"description":"Cleavage; by factor I","evidences":[{"source":"PubMed","id":"28671664","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
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_FI9
Number of Residues4
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_FI10
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues8
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_FI12
Number of Residues260
DetailsDomain: {"description":"Sushi 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues236
DetailsDomain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues228
DetailsDomain: {"description":"Sushi 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues796
DetailsDomain: {"description":"VWFA","evidences":[{"source":"PROSITE-ProRule","id":"PRU00219","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues12
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"10637221","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15016353","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q0P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues8
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_FI19
Number of Residues4
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_FI20
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"2006911","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues4
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

239492

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