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5O32

The structure of complement complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004866molecular_functionendopeptidase inhibitor activity
B0004866molecular_functionendopeptidase inhibitor activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
D0016020cellular_componentmembrane
E0004866molecular_functionendopeptidase inhibitor activity
F0004866molecular_functionendopeptidase inhibitor activity
F0005576cellular_componentextracellular region
F0005615cellular_componentextracellular space
H0016020cellular_componentmembrane
I0004252molecular_functionserine-type endopeptidase activity
I0006508biological_processproteolysis
J0004252molecular_functionserine-type endopeptidase activity
J0006508biological_processproteolysis
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ILEU376-CYS381

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAckGDSGGPLV
ChainResidueDetails
IASP519-VAL530

site_idPS00477
Number of Residues9
DetailsALPHA_2_MACROGLOBULIN Alpha-2-macroglobulin family thiolester region signature. PsGCGEQnM
ChainResidueDetails
BPRO1007-MET1015

site_idPS01209
Number of Residues23
DetailsLDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIpsqyq.CNgevDCitg.EDEvg...C
ChainResidueDetails
DCYS271-CYS293

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSite: {"description":"(Microbial infection) Cleavage; by S.pyogenes SpeB","evidences":[{"source":"PubMed","id":"18160402","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
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 Residues32
DetailsPeptide: {"description":"Complement C3f fragment","featureId":"PRO_0000005916","evidences":[{"source":"PubMed","id":"8376604","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues286
DetailsDomain: {"description":"NTR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00295","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues38
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues50
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_FI8
Number of Residues6
DetailsSite: {"description":"Cleavage; by factor I","evidences":[{"source":"PubMed","id":"28671664","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
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_FI10
Number of Residues2
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_FI11
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
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_FI13
Number of Residues126
DetailsDomain: {"description":"Sushi 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues120
DetailsDomain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues126
DetailsDomain: {"description":"Sushi 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues112
DetailsDomain: {"description":"Sushi 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues106
DetailsDomain: {"description":"Kazal-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00798","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues196
DetailsDomain: {"description":"SRCR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00196","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues88
DetailsDomain: {"description":"LDL-receptor class A 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues72
DetailsDomain: {"description":"LDL-receptor class A 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21768352","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XRC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21768352","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XRC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21768352","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XRC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues468
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"P00750","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21768352","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XRC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21768352","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XRC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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