4E0S
Crystal Structure of C5b-6
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004866 | molecular_function | endopeptidase inhibitor activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0006954 | biological_process | inflammatory response |
| A | 0006956 | biological_process | complement activation |
| B | 0001701 | biological_process | in utero embryonic development |
| B | 0002376 | biological_process | immune system process |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005579 | cellular_component | membrane attack complex |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006955 | biological_process | immune response |
| B | 0006956 | biological_process | complement activation |
| B | 0006958 | biological_process | complement activation, classical pathway |
| B | 0016020 | cellular_component | membrane |
| B | 0031640 | biological_process | killing of cells of another organism |
| B | 0044218 | cellular_component | other organism cell membrane |
| B | 0045087 | biological_process | innate immune response |
| B | 0050778 | biological_process | positive regulation of immune response |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0160257 | biological_process | complement activation, GZMK pathway |
| B | 1902495 | cellular_component | transmembrane transporter complex |
Functional Information from PROSITE/UniProt
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CvCqsGtyGEnC |
| Chain | Residue | Details |
| B | CYS520-CYS531 |
| site_id | PS00279 |
| Number of Residues | 12 |
| Details | MACPF_1 Membrane attack complex/perforin (MACPF) domain signature. YsrifddFGTHY |
| Chain | Residue | Details |
| B | TYR333-TYR344 |
| site_id | PS01177 |
| Number of Residues | 35 |
| Details | ANAPHYLATOXIN_1 Anaphylatoxin domain signature. CCydGacvnnde.TCEqraarisl.GprCikafte.CC |
| Chain | Residue | Details |
| A | CYS698-CYS732 |
| site_id | PS01209 |
| Number of Residues | 23 |
| Details | LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIarkle.CNgenDCgdn.SDErd...C |
| Chain | Residue | Details |
| B | CYS130-CYS152 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 144 |
| Details | Domain: {"description":"NTR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00295","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | Region: {"description":"Involved in the tick complement inhibitor CirpT1","evidences":[{"source":"PubMed","id":"31871188","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Glycosylation: {"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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 13 |
| Details | Transmembrane: {"description":"Beta stranded","evidences":[{"source":"PubMed","id":"30552328","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6H04","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 57 |
| Details | Domain: {"description":"TSP type-1 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 53 |
| Details | Domain: {"description":"TSP type-1 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 37 |
| Details | Domain: {"description":"LDL-receptor class A","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 30 |
| Details | Domain: {"description":"EGF-like"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 47 |
| Details | Domain: {"description":"TSP type-1 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 59 |
| Details | Domain: {"description":"Sushi 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 61 |
| Details | Domain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 59 |
| Details | Domain: {"description":"Kazal-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00798","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 58 |
| Details | Domain: {"description":"Kazal-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00798","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 77 |
| Details | Region: {"description":"CCP 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 76 |
| Details | Region: {"description":"CCP 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 76 |
| Details | Region: {"description":"Factor I module (FIM) 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22500023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4E0S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"C-linked (Man) tryptophan","evidences":[{"source":"PubMed","id":"10551839","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 5 |
| Details | Glycosylation: {"description":"C-linked (Man) tryptophan; partial","evidences":[{"source":"PubMed","id":"10551839","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"O-linked (Fuc...) threonine","evidences":[{"source":"PubMed","id":"22267737","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22267737","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
