3PVM
Structure of Complement C5 in Complex with CVF
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 | 0004866 | molecular_function | endopeptidase inhibitor activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0006954 | biological_process | inflammatory response |
| B | 0006956 | biological_process | complement activation |
| C | 0004866 | molecular_function | endopeptidase inhibitor activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005615 | cellular_component | extracellular space |
| C | 0006954 | biological_process | inflammatory response |
| C | 0006956 | biological_process | complement activation |
| D | 0004866 | molecular_function | endopeptidase inhibitor activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005615 | cellular_component | extracellular space |
| D | 0006954 | biological_process | inflammatory response |
| D | 0006956 | biological_process | complement activation |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DDNEDGFIAdsDI |
| Chain | Residue | Details |
| B | ASP733-ILE745 |
| site_id | PS00477 |
| Number of Residues | 9 |
| Details | ALPHA_2_MACROGLOBULIN Alpha-2-macroglobulin family thiolester region signature. PsGCGEQnM |
| Chain | Residue | Details |
| B | PRO990-MET998 |
| site_id | PS01177 |
| Number of Residues | 35 |
| Details | ANAPHYLATOXIN_1 Anaphylatoxin domain signature. CCydGacvnnde.TCEqraarisl.GprCikafte.CC |
| Chain | Residue | Details |
| A | CYS698-CYS732 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 68 |
| Details | Domain: {"description":"Anaphylatoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00022","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 574 |
| Details | Domain: {"description":"NTR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00295","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 52 |
| 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_FI4 |
| Number of Residues | 58 |
| Details | Region: {"description":"Involved in C5AR1 binding","evidences":[{"source":"PubMed","id":"9553099","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Cleavage; by C5 convertase","evidences":[{"source":"PubMed","id":"6554279","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18536718","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_FI7 |
| Number of Residues | 2 |
| 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_FI8 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| 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_FI10 |
| Number of Residues | 22 |
| Details | Region: {"description":"Factor B binding site","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19574954","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21217642","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
