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3T5O

Crystal Structure of human Complement Component C6

Functional Information from GO Data
ChainGOidnamespacecontents
A0001701biological_processin utero embryonic development
A0001970biological_processpositive regulation of activation of membrane attack complex
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
A0006958biological_processcomplement activation, classical pathway
A0022829molecular_functionwide pore channel activity
A0031640biological_processkilling of cells of another organism
A0044218cellular_componentother organism cell membrane
A0045087biological_processinnate immune response
A0045766biological_processpositive regulation of angiogenesis
A0045917biological_processpositive regulation of complement activation
A0050778biological_processpositive regulation of immune response
A0055085biological_processtransmembrane transport
A0070062cellular_componentextracellular exosome
A0160257biological_processcomplement activation, GZMK pathway
Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CvCqsGtyGEnC
ChainResidueDetails
ACYS520-CYS531

site_idPS00279
Number of Residues12
DetailsMACPF_1 Membrane attack complex/perforin (MACPF) domain signature. YsrifddFGTHY
ChainResidueDetails
ATYR333-TYR344

site_idPS01209
Number of Residues23
DetailsLDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIarkle.CNgenDCgdn.SDErd...C
ChainResidueDetails
ACYS130-CYS152

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues13
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 Residues57
DetailsDomain: {"description":"TSP type-1 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues53
DetailsDomain: {"description":"TSP type-1 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues37
DetailsDomain: {"description":"LDL-receptor class A","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues30
DetailsDomain: {"description":"EGF-like"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues47
DetailsDomain: {"description":"TSP type-1 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues59
DetailsDomain: {"description":"Sushi 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues61
DetailsDomain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues59
DetailsDomain: {"description":"Kazal-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00798","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues58
DetailsDomain: {"description":"Kazal-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00798","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues76
DetailsRegion: {"description":"CCP 2"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues76
DetailsRegion: {"description":"Factor I module (FIM) 2"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22500023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4E0S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsGlycosylation: {"description":"C-linked (Man) tryptophan","evidences":[{"source":"PubMed","id":"10551839","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues5
DetailsGlycosylation: {"description":"C-linked (Man) tryptophan; partial","evidences":[{"source":"PubMed","id":"10551839","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (Fuc...) threonine","evidences":[{"source":"PubMed","id":"22267737","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI17
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_FI18
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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