8WYR
Cryo-EM structure of human CD5L bound to IgM-Fc/J
Functional Information from GO Data
Chain | GOid | namespace | contents |
M | 0002376 | biological_process | immune system process |
M | 0005576 | cellular_component | extracellular region |
M | 0005615 | cellular_component | extracellular space |
M | 0005737 | cellular_component | cytoplasm |
M | 0005886 | cellular_component | plasma membrane |
M | 0006915 | biological_process | apoptotic process |
M | 0006954 | biological_process | inflammatory response |
M | 0006968 | biological_process | cellular defense response |
M | 0009986 | cellular_component | cell surface |
M | 0016020 | cellular_component | membrane |
M | 0030449 | biological_process | regulation of complement activation |
M | 0072562 | cellular_component | blood microparticle |
M | 1903661 | biological_process | positive regulation of complement-dependent cytotoxicity |
Functional Information from PROSITE/UniProt
site_id | PS00290 |
Number of Residues | 7 |
Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. FTCRVDH |
Chain | Residue | Details |
A | PHE318-HIS324 | |
A | PHE424-HIS430 | |
A | TYR534-HIS540 |
site_id | PS00420 |
Number of Residues | 38 |
Details | SRCR_1 SRCR domain signature. GlhrceGrvEveqkgqWGtvCddgWdikdvavlCrelG |
Chain | Residue | Details |
M | GLY29-GLY66 | |
M | GLY249-GLY286 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 900 |
Details | Domain: {"description":"Ig-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1010 |
Details | Domain: {"description":"Ig-like 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"35981043","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4742735","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7XQ8","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 10 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35981043","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4742735","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7XQ8","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000167","evidences":[{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18780401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 101 |
Details | Domain: {"description":"SRCR 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00196","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |