Functional Information from GO Data
Chain | GOid | namespace | contents |
C | 0005509 | molecular_function | calcium ion binding |
D | 0005509 | molecular_function | calcium ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00010 |
Number of Residues | 12 |
Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CtNsegaFqCwC |
Chain | Residue | Details |
C | CYS409-CYS420 | |
site_id | PS01186 |
Number of Residues | 16 |
Details | EGF_2 EGF-like domain signature 2. CwCeaGYelrpdrrsC |
Chain | Residue | Details |
C | CYS418-CYS433 | |
C | CYS722-CYS736 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 84 |
Details | Repeat: {"description":"LDL-receptor class B 1"} |
site_id | SWS_FT_FI2 |
Number of Residues | 84 |
Details | Repeat: {"description":"LDL-receptor class B 2"} |
site_id | SWS_FT_FI3 |
Number of Residues | 86 |
Details | Repeat: {"description":"LDL-receptor class B 3"} |
site_id | SWS_FT_FI4 |
Number of Residues | 84 |
Details | Repeat: {"description":"LDL-receptor class B 4"} |
site_id | SWS_FT_FI5 |
Number of Residues | 80 |
Details | Repeat: {"description":"LDL-receptor class B 5"} |
site_id | SWS_FT_FI6 |
Number of Residues | 78 |
Details | Domain: {"description":"EGF-like 3"} |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PDB","id":"3V64","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3V65","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PDB","id":"3V64","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | Site: {"description":"Alternative splice site to produce 'z' isoforms"} |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | Site: {"description":"Highly important for the agrin receptor complex activity of the 'z(8)' insert"} |