9BDT
Apolipoprotein B 100 bound to LDL receptor and legobody
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005319 | molecular_function | lipid transporter activity |
| A | 0006869 | biological_process | lipid transport |
| B | 0005515 | molecular_function | protein binding |
| B | 0005618 | cellular_component | cell wall |
| B | 0006974 | biological_process | DNA damage response |
| B | 0008643 | biological_process | carbohydrate transport |
| B | 0015144 | molecular_function | carbohydrate transmembrane transporter activity |
| B | 0015768 | biological_process | maltose transport |
| B | 0016020 | cellular_component | membrane |
| B | 0019865 | molecular_function | immunoglobulin binding |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0034219 | biological_process | carbohydrate transmembrane transport |
| B | 0034289 | biological_process | detection of maltose stimulus |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0042956 | biological_process | maltodextrin transmembrane transport |
| B | 0043190 | cellular_component | ATP-binding cassette (ABC) transporter complex |
| B | 0055052 | cellular_component | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing |
| B | 0055085 | biological_process | transmembrane transport |
| B | 0060326 | biological_process | cell chemotaxis |
| B | 1901982 | molecular_function | maltose binding |
| B | 1990060 | cellular_component | maltose transport complex |
| I | 0005509 | molecular_function | calcium ion binding |
| R | 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. CnDlkigYeClC |
| Chain | Residue | Details |
| I | CYS329-CYS340 | |
| I | CYS368-CYS379 |
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH |
| Chain | Residue | Details |
| L | TYR197-HIS203 | |
| H | TYR204-HIS210 |
| site_id | PS01037 |
| Number of Residues | 18 |
| Details | SBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN |
| Chain | Residue | Details |
| B | PRO109-ASN126 |
| site_id | PS01186 |
| Number of Residues | 15 |
| Details | EGF_2 EGF-like domain signature 2. ClCpdGFqlvaqrr.C |
| Chain | Residue | Details |
| I | CYS338-CYS352 | |
| I | CYS377-CYS392 |
| site_id | PS01187 |
| Number of Residues | 24 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DiDECqdpdt.........Csql....CvNleggYkC |
| Chain | Residue | Details |
| I | ASP354-CYS377 |
| site_id | PS01209 |
| Number of Residues | 25 |
| Details | LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIsykwv.CDgsaECqdg.SDEsqet.C |
| Chain | Residue | Details |
| I | CYS39-CYS63 | |
| I | CYS82-CYS104 | |
| I | CYS121-CYS143 | |
| I | CYS160-CYS184 | |
| I | CYS209-CYS231 | |
| I | CYS248-CYS270 | |
| I | CYS289-CYS313 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 626 |
| Details | Domain: {"description":"Vitellogenin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00557","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 339 |
| Details | Region: {"description":"Heparin-binding"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Region: {"description":"Basic (possible receptor binding region)"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Region: {"description":"LDL receptor binding"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"10679026","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 5 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 54 |
| Details | Repeat: {"description":"2-2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 42 |
| Details | Repeat: {"description":"LDL-receptor class B 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 43 |
| Details | Repeat: {"description":"LDL-receptor class B 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 42 |
| Details | Repeat: {"description":"LDL-receptor class B 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 42 |
| Details | Repeat: {"description":"LDL-receptor class B 6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| 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 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 39 |
| Details | Domain: {"description":"LDL-receptor class A 7","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 39 |
| Details | Domain: {"description":"EGF-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19520913","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






