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3OJY

Crystal Structure of Human Complement Component C8

Functional Information from GO Data
ChainGOidnamespacecontents
A0001848molecular_functioncomplement binding
A0002376biological_processimmune system process
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005579cellular_componentmembrane attack complex
A0005615cellular_componentextracellular space
A0005886cellular_componentplasma membrane
A0006955biological_processimmune response
A0006956biological_processcomplement activation
A0006957biological_processcomplement activation, alternative pathway
A0006958biological_processcomplement activation, classical pathway
A0016020cellular_componentmembrane
A0022829molecular_functionwide pore channel activity
A0031640biological_processkilling of cells of another organism
A0044218cellular_componentother organism cell membrane
A0044877molecular_functionprotein-containing complex binding
A0045087biological_processinnate immune response
A0050778biological_processpositive regulation of immune response
A0055085biological_processtransmembrane transport
A0070062cellular_componentextracellular exosome
A0072562cellular_componentblood microparticle
A0160257biological_processcomplement activation, GZMK pathway
B0002376biological_processimmune system process
B0005576cellular_componentextracellular region
B0005579cellular_componentmembrane attack complex
B0005615cellular_componentextracellular space
B0005886cellular_componentplasma membrane
B0006955biological_processimmune response
B0006956biological_processcomplement activation
B0006957biological_processcomplement activation, alternative pathway
B0006958biological_processcomplement activation, classical pathway
B0016020cellular_componentmembrane
B0022829molecular_functionwide pore channel activity
B0031640biological_processkilling of cells of another organism
B0044218cellular_componentother organism cell membrane
B0044877molecular_functionprotein-containing complex binding
B0045087biological_processinnate immune response
B0050778biological_processpositive regulation of immune response
B0055085biological_processtransmembrane transport
B0070062cellular_componentextracellular exosome
B0160257biological_processcomplement activation, GZMK pathway
B1903561cellular_componentextracellular vesicle
C0002376biological_processimmune system process
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005579cellular_componentmembrane attack complex
C0005886cellular_componentplasma membrane
C0006956biological_processcomplement activation
C0006957biological_processcomplement activation, alternative pathway
C0006958biological_processcomplement activation, classical pathway
C0019841molecular_functionretinol binding
C0022829molecular_functionwide pore channel activity
C0031640biological_processkilling of cells of another organism
C0044218cellular_componentother organism cell membrane
C0045087biological_processinnate immune response
C0050778biological_processpositive regulation of immune response
C0055085biological_processtransmembrane transport
C0070062cellular_componentextracellular exosome
C0072562cellular_componentblood microparticle
C0160257biological_processcomplement activation, GZMK pathway
Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CqCrlGslGAaC
ChainResidueDetails
ACYS487-CYS498
BCYS469-CYS480

site_idPS00213
Number of Residues14
DetailsLIPOCALIN Lipocalin signature. NFDaqQFAGTWLLV
ChainResidueDetails
CASN21-VAL34

site_idPS00279
Number of Residues12
DetailsMACPF_1 Membrane attack complex/perforin (MACPF) domain signature. YakfindYGTHY
ChainResidueDetails
ATYR300-TYR311
BTYR279-TYR290

site_idPS01209
Number of Residues23
DetailsLDLRA_1 LDL-receptor class A (LDLRA) domain signature. CLkrhlv.CNgdqDCldgsDEDd....C
ChainResidueDetails
ACYS78-CYS100
BCYS79-CYS101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsTransmembrane: {"description":"Beta stranded","evidences":[{"source":"PubMed","id":"30552328","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6H04","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues75
DetailsDomain: {"description":"LDL-receptor class A","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues60
DetailsDomain: {"description":"EGF-like"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21454577","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3OJY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Not glycosylated"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsGlycosylation: {"description":"C-linked (Man) tryptophan","evidences":[{"source":"PubMed","id":"10551839","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues53
DetailsDomain: {"description":"TSP type-1 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21454577","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30552328","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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