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4A5W

Crystal structure of C5b6

Functional Information from GO Data
ChainGOidnamespacecontents
A0001664molecular_functionG protein-coupled receptor binding
A0002376biological_processimmune system process
A0002682biological_processregulation of immune system process
A0004866molecular_functionendopeptidase inhibitor activity
A0005102molecular_functionsignaling receptor binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005579cellular_componentmembrane attack complex
A0005615cellular_componentextracellular space
A0006935biological_processchemotaxis
A0006954biological_processinflammatory response
A0006957biological_processcomplement activation, alternative pathway
A0006958biological_processcomplement activation, classical pathway
A0007166biological_processcell surface receptor signaling pathway
A0007186biological_processG protein-coupled receptor signaling pathway
A0008009molecular_functionchemokine activity
A0010575biological_processpositive regulation of vascular endothelial growth factor production
A0010760biological_processnegative regulation of macrophage chemotaxis
A0016477biological_processcell migration
A0031640biological_processkilling of cells of another organism
A0032722biological_processpositive regulation of chemokine production
A0044218cellular_componentother organism cell membrane
A0045087biological_processinnate immune response
A0050920biological_processregulation of chemotaxis
A0060326biological_processcell chemotaxis
A0070062cellular_componentextracellular exosome
A0160257biological_processcomplement activation, GZMK pathway
B0001970biological_processpositive regulation of activation of membrane attack complex
B0002376biological_processimmune system process
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005579cellular_componentmembrane attack complex
B0005615cellular_componentextracellular space
B0005886cellular_componentplasma membrane
B0006955biological_processimmune response
B0006956biological_processcomplement activation
B0006958biological_processcomplement activation, classical pathway
B0022829molecular_functionwide pore channel activity
B0031640biological_processkilling of cells of another organism
B0044218cellular_componentother organism cell membrane
B0045087biological_processinnate immune response
B0045766biological_processpositive regulation of angiogenesis
B0045917biological_processpositive regulation of complement activation
B0050778biological_processpositive regulation of immune response
B0055085biological_processtransmembrane transport
B0070062cellular_componentextracellular exosome
B0160257biological_processcomplement activation, GZMK pathway
Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CvCqsGtyGEnC
ChainResidueDetails
BCYS541-CYS552

site_idPS00279
Number of Residues12
DetailsMACPF_1 Membrane attack complex/perforin (MACPF) domain signature. YsrifddFGTHY
ChainResidueDetails
BTYR354-TYR365

site_idPS01209
Number of Residues23
DetailsLDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIarkle.CNgenDCgdn.SDErd...C
ChainResidueDetails
BCYS151-CYS173

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues144
DetailsDomain: {"description":"NTR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00295","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues26
DetailsRegion: {"description":"Involved in the tick complement inhibitor CirpT1","evidences":[{"source":"PubMed","id":"31871188","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
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_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsTransmembrane: {"description":"Beta stranded","evidences":[{"source":"PubMed","id":"30552328","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6H04","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues57
DetailsDomain: {"description":"TSP type-1 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues53
DetailsDomain: {"description":"TSP type-1 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues37
DetailsDomain: {"description":"LDL-receptor class A","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues30
DetailsDomain: {"description":"EGF-like"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues47
DetailsDomain: {"description":"TSP type-1 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues59
DetailsDomain: {"description":"Sushi 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues61
DetailsDomain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues59
DetailsDomain: {"description":"Kazal-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00798","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues58
DetailsDomain: {"description":"Kazal-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00798","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues77
DetailsRegion: {"description":"CCP 1"}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues292
DetailsRegion: {"description":"C5b-binding domain"}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues76
DetailsRegion: {"description":"CCP 2"}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues74
DetailsRegion: {"description":"Factor I module (FIM) 1"}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues76
DetailsRegion: {"description":"Factor I module (FIM) 2"}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22500023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4E0S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues1
DetailsGlycosylation: {"description":"C-linked (Man) tryptophan","evidences":[{"source":"PubMed","id":"10551839","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues5
DetailsGlycosylation: {"description":"C-linked (Man) tryptophan; partial","evidences":[{"source":"PubMed","id":"10551839","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (Fuc...) threonine","evidences":[{"source":"PubMed","id":"22267737","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI25
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

247536

PDB entries from 2026-01-14

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