3P5B
The structure of the LDLR/PCSK9 complex reveals the receptor in an extended conformation
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA L 1 |
| Chain | Residue |
| L | ASP333 |
| L | ILE334 |
| L | LEU350 |
| L | GLY353 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 2 |
| Chain | Residue |
| A | ASP360 |
| A | ALA328 |
| A | ALA330 |
| A | VAL333 |
| A | THR335 |
| A | CYS358 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA L 3 |
| Chain | Residue |
| L | GLU296 |
| L | ASP310 |
Functional Information from PROSITE/UniProt
| site_id | PS00010 |
| Number of Residues | 12 |
| Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CnDlkigYeClC |
| Chain | Residue | Details |
| L | CYS308-CYS319 | |
| L | CYS347-CYS358 |
| site_id | PS01186 |
| Number of Residues | 15 |
| Details | EGF_2 EGF-like domain signature 2. ClCpdGFqlvaqrr.C |
| Chain | Residue | Details |
| L | CYS317-CYS331 | |
| L | CYS356-CYS371 |
| site_id | PS01187 |
| Number of Residues | 24 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DiDECqdpdt.........Csql....CvNleggYkC |
| Chain | Residue | Details |
| L | ASP333-CYS356 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 72 |
| Details | Domain: {"description":"Inhibitor I9","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16912035","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 39 |
| Details | Domain: {"description":"EGF-like 2; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 41 |
| Details | Repeat: {"description":"LDL-receptor class B 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 42 |
| Details | Repeat: {"description":"LDL-receptor class B 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 43 |
| Details | Repeat: {"description":"LDL-receptor class B 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 42 |
| Details | Repeat: {"description":"LDL-receptor class B 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 42 |
| Details | Repeat: {"description":"LDL-receptor class B 6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 49 |
| Details | Domain: {"description":"EGF-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
