Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8B0F

CryoEM structure of C5b8-CD59

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0004866molecular_functionendopeptidase inhibitor activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006954biological_processinflammatory response
A0006956biological_processcomplement activation
B0005579cellular_componentmembrane attack complex
B0006955biological_processimmune response
C0005579cellular_componentmembrane attack complex
C0006955biological_processimmune response
D0005579cellular_componentmembrane attack complex
D0006955biological_processimmune response
E0005579cellular_componentmembrane attack complex
E0006955biological_processimmune response
F0005579cellular_componentmembrane attack complex
F0006956biological_processcomplement activation
Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CiCpvGsqGLaC
ChainResidueDetails
DCYS469-CYS480
CCYS475-CYS486
BCYS541-CYS552
ECYS487-CYS498
site_idPS00213
Number of Residues14
DetailsLIPOCALIN Lipocalin signature. NFDaqQFAGTWLLV
ChainResidueDetails
FASN21-VAL34
site_idPS00279
Number of Residues12
DetailsMACPF_1 Membrane attack complex/perforin (MACPF) domain signature. YrdlfrdFGTHY
ChainResidueDetails
DTYR279-TYR290
CTYR292-TYR303
BTYR354-TYR365
ETYR300-TYR311
site_idPS00983
Number of Residues44
DetailsLY6_UPAR Ly-6 / u-PAR domain signature. QCYnCpnptad..Cktav....NCSsdfdaClitkaglqvynkcwkfeh......C
ChainResidueDetails
GGLN2-CYS45
site_idPS01177
Number of Residues35
DetailsANAPHYLATOXIN_1 Anaphylatoxin domain signature. CCydGacvnnde.TCEqraarisl.GprCikafte.CC
ChainResidueDetails
ACYS698-CYS732
site_idPS01186
Number of Residues16
DetailsEGF_2 EGF-like domain signature 2. CvCkmPYecgpsldvC
ChainResidueDetails
CCYS713-CYS728
site_idPS01209
Number of Residues23
DetailsLDLRA_1 LDL-receptor class A (LDLRA) domain signature. CVnrrll.CNgdnDCgdq.SDEan...C
ChainResidueDetails
DCYS79-CYS101
CCYS96-CYS119
BCYS151-CYS173
ECYS78-CYS100
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues26
DetailsRegion: {"description":"Involved in the tick complement inhibitor CirpT1","evidences":[{"source":"PubMed","id":"31871188","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18536718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21217642","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CU7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KLS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KM9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues216
DetailsDomain: {"description":"TSP type-1 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues146
DetailsDomain: {"description":"TSP type-1 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues150
DetailsDomain: {"description":"LDL-receptor class A","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues120
DetailsDomain: {"description":"EGF-like"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues47
DetailsDomain: {"description":"TSP type-1 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues118
DetailsDomain: {"description":"Sushi 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues122
DetailsDomain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues147
DetailsRegion: {"description":"CCP 1"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22500023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4E0S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues10
DetailsGlycosylation: {"description":"C-linked (Man) tryptophan","evidences":[{"source":"PubMed","id":"10551839","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues8
DetailsGlycosylation: {"description":"C-linked (Man) tryptophan; partial","evidences":[{"source":"PubMed","id":"10551839","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (Fuc...) threonine","evidences":[{"source":"PubMed","id":"22267737","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22267737","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues332
DetailsDomain: {"description":"MACPF","evidences":[{"source":"PROSITE-ProRule","id":"PRU00745","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues100
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues12
DetailsCompositional bias: {"description":"Acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues11
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues9
DetailsCompositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21454577","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3OJY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21454577","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
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
site_idSWS_FT_FI26
Number of Residues1
DetailsSite: {"description":"Not glycosylated"}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsLipidation: {"description":"GPI-anchor amidated asparagine","evidences":[{"source":"PubMed","id":"17566972","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8276756","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18780401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8670172","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"10805801","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GalNAc...) threonine","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon