6L47
Structure of the human sterol O-acyltransferase 1 in complex with CI-976
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008374 | molecular_function | O-acyltransferase activity |
A | 0016020 | cellular_component | membrane |
A | 0034736 | molecular_function | cholesterol O-acyltransferase activity |
A | 0042632 | biological_process | cholesterol homeostasis |
B | 0008374 | molecular_function | O-acyltransferase activity |
B | 0016020 | cellular_component | membrane |
B | 0034736 | molecular_function | cholesterol O-acyltransferase activity |
B | 0042632 | biological_process | cholesterol homeostasis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue E5L A 1001 |
Chain | Residue |
A | TYR416 |
A | TYR417 |
A | TRP420 |
A | ASN421 |
A | VAL424 |
A | HIS460 |
A | ASN511 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue CLR A 1002 |
Chain | Residue |
A | PHE145 |
A | ILE146 |
A | CYS333 |
A | TYR336 |
A | PHE378 |
A | LEU379 |
A | PHE382 |
A | TRP408 |
B | HIS137 |
B | THR140 |
B | ILE141 |
A | ILE138 |
A | TYR142 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue E5L B 1001 |
Chain | Residue |
B | TYR416 |
B | TYR417 |
B | TRP420 |
B | ASN421 |
B | VAL424 |
B | HIS460 |
B | ASN511 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue CLR B 1002 |
Chain | Residue |
A | HIS137 |
A | THR140 |
A | ILE141 |
B | ILE138 |
B | TYR142 |
B | PHE145 |
B | ILE146 |
B | CYS333 |
B | TYR336 |
B | PHE378 |
B | LEU379 |
B | PHE382 |
B | TRP408 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:32433614, ECO:0000305|PubMed:32433613, ECO:0007744|PDB:6P2J, ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM |
Chain | Residue | Details |
A | ARG139-ASP160 | |
B | ARG139-ASP160 |
site_id | SWS_FT_FI2 |
Number of Residues | 136 |
Details | TOPO_DOM: Lumenal => ECO:0000305 |
Chain | Residue | Details |
A | TYR161-LYS180 | |
B | PRO529-PHE552 | |
A | ALA245-SER252 | |
A | LYS353-SER369 | |
A | SER469-VAL474 | |
A | PRO529-PHE552 | |
B | TYR161-LYS180 | |
B | ALA245-SER252 | |
B | LYS353-SER369 | |
B | SER469-VAL474 |
site_id | SWS_FT_FI3 |
Number of Residues | 50 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:32433614, ECO:0000305|PubMed:32433613, ECO:0007744|PDB:6P2J, ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM |
Chain | Residue | Details |
A | PHE181-TRP206 | |
B | PHE181-TRP206 |
site_id | SWS_FT_FI4 |
Number of Residues | 210 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
Chain | Residue | Details |
A | ALA207-ILE218 | |
A | ARG277-ARG319 | |
A | LEU396-ARG443 | |
A | ASN491-LYS496 | |
B | ALA207-ILE218 | |
B | ARG277-ARG319 | |
B | LEU396-ARG443 | |
B | ASN491-LYS496 |
site_id | SWS_FT_FI5 |
Number of Residues | 50 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:32433614, ECO:0000305|PubMed:32433613, ECO:0007744|PDB:6P2J, ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM |
Chain | Residue | Details |
A | ARG219-LEU244 | |
B | ARG219-LEU244 |
site_id | SWS_FT_FI6 |
Number of Residues | 46 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:32433614, ECO:0000305|PubMed:32433613, ECO:0007744|PDB:6P2J, ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM |
Chain | Residue | Details |
A | ARG253-PRO276 | |
B | ARG253-PRO276 |
site_id | SWS_FT_FI7 |
Number of Residues | 64 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:32433614, ECO:0000305|PubMed:32433613, ECO:0007744|PDB:6P2J, ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM |
Chain | Residue | Details |
A | TRP320-ILE352 | |
B | TRP320-ILE352 |
site_id | SWS_FT_FI8 |
Number of Residues | 50 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:32433614, ECO:0000305|PubMed:32433613, ECO:0007744|PDB:6P2J, ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM |
Chain | Residue | Details |
A | ILE370-MET395 | |
B | ILE370-MET395 |
site_id | SWS_FT_FI9 |
Number of Residues | 48 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:32433614, ECO:0000305|PubMed:32433613, ECO:0007744|PDB:6P2J, ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM |
Chain | Residue | Details |
A | PHE444-LEU468 | |
B | PHE444-LEU468 |
site_id | SWS_FT_FI10 |
Number of Residues | 30 |
Details | TRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:32433614, ECO:0000305|PubMed:32433613, ECO:0007744|PDB:6P2J, ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM |
Chain | Residue | Details |
A | LEU475-VAL490 | |
B | LEU475-VAL490 |
site_id | SWS_FT_FI11 |
Number of Residues | 62 |
Details | TRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:32433613, ECO:0000269|PubMed:32433614, ECO:0007744|PDB:6P2J, ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM |
Chain | Residue | Details |
A | PRO497-CYS528 | |
B | PRO497-CYS528 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:16154994, ECO:0000269|PubMed:16647063, ECO:0000269|PubMed:32433613, ECO:0000269|PubMed:32433614, ECO:0007744|PDB:6VUM |
Chain | Residue | Details |
A | HIS460 | |
B | HIS460 |
site_id | SWS_FT_FI13 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:32433613, ECO:0007744|PDB:6VUM |
Chain | Residue | Details |
A | HIS137 | |
A | ARG418 | |
A | TYR433 | |
A | SER456 | |
B | HIS137 | |
B | ARG418 | |
B | TYR433 | |
B | SER456 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:32433614, ECO:0007744|PDB:6P2P |
Chain | Residue | Details |
A | ASN415 | |
B | ASN415 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:32433614, ECO:0007744|PDB:6P2J |
Chain | Residue | Details |
A | ASN421 | |
B | ASN421 |
site_id | SWS_FT_FI16 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:32433613, ECO:0000269|PubMed:32433614, ECO:0007744|PDB:6P2J, ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM |
Chain | Residue | Details |
A | HIS425 | |
A | LYS445 | |
B | HIS425 | |
B | LYS445 |