6VUM
Structure of nevanimibe-bound human tetrameric ACAT1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000062 | molecular_function | fatty-acyl-CoA binding |
| A | 0004772 | molecular_function | sterol O-acyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0008374 | molecular_function | O-acyltransferase activity |
| A | 0010742 | biological_process | macrophage derived foam cell differentiation |
| A | 0010878 | biological_process | cholesterol storage |
| A | 0015485 | molecular_function | cholesterol binding |
| A | 0016020 | cellular_component | membrane |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0033344 | biological_process | cholesterol efflux |
| A | 0034379 | biological_process | very-low-density lipoprotein particle assembly |
| A | 0034383 | biological_process | low-density lipoprotein particle clearance |
| A | 0034736 | molecular_function | cholesterol O-acyltransferase activity |
| A | 0042632 | biological_process | cholesterol homeostasis |
| A | 0042986 | biological_process | positive regulation of amyloid precursor protein biosynthetic process |
| B | 0000062 | molecular_function | fatty-acyl-CoA binding |
| B | 0004772 | molecular_function | sterol O-acyltransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0008203 | biological_process | cholesterol metabolic process |
| B | 0008374 | molecular_function | O-acyltransferase activity |
| B | 0010742 | biological_process | macrophage derived foam cell differentiation |
| B | 0010878 | biological_process | cholesterol storage |
| B | 0015485 | molecular_function | cholesterol binding |
| B | 0016020 | cellular_component | membrane |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0033344 | biological_process | cholesterol efflux |
| B | 0034379 | biological_process | very-low-density lipoprotein particle assembly |
| B | 0034383 | biological_process | low-density lipoprotein particle clearance |
| B | 0034736 | molecular_function | cholesterol O-acyltransferase activity |
| B | 0042632 | biological_process | cholesterol homeostasis |
| B | 0042986 | biological_process | positive regulation of amyloid precursor protein biosynthetic process |
| C | 0000062 | molecular_function | fatty-acyl-CoA binding |
| C | 0004772 | molecular_function | sterol O-acyltransferase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0005789 | cellular_component | endoplasmic reticulum membrane |
| C | 0008203 | biological_process | cholesterol metabolic process |
| C | 0008374 | molecular_function | O-acyltransferase activity |
| C | 0010742 | biological_process | macrophage derived foam cell differentiation |
| C | 0010878 | biological_process | cholesterol storage |
| C | 0015485 | molecular_function | cholesterol binding |
| C | 0016020 | cellular_component | membrane |
| C | 0016746 | molecular_function | acyltransferase activity |
| C | 0033344 | biological_process | cholesterol efflux |
| C | 0034379 | biological_process | very-low-density lipoprotein particle assembly |
| C | 0034383 | biological_process | low-density lipoprotein particle clearance |
| C | 0034736 | molecular_function | cholesterol O-acyltransferase activity |
| C | 0042632 | biological_process | cholesterol homeostasis |
| C | 0042986 | biological_process | positive regulation of amyloid precursor protein biosynthetic process |
| D | 0000062 | molecular_function | fatty-acyl-CoA binding |
| D | 0004772 | molecular_function | sterol O-acyltransferase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0005789 | cellular_component | endoplasmic reticulum membrane |
| D | 0008203 | biological_process | cholesterol metabolic process |
| D | 0008374 | molecular_function | O-acyltransferase activity |
| D | 0010742 | biological_process | macrophage derived foam cell differentiation |
| D | 0010878 | biological_process | cholesterol storage |
| D | 0015485 | molecular_function | cholesterol binding |
| D | 0016020 | cellular_component | membrane |
| D | 0016746 | molecular_function | acyltransferase activity |
| D | 0033344 | biological_process | cholesterol efflux |
| D | 0034379 | biological_process | very-low-density lipoprotein particle assembly |
| D | 0034383 | biological_process | low-density lipoprotein particle clearance |
| D | 0034736 | molecular_function | cholesterol O-acyltransferase activity |
| D | 0042632 | biological_process | cholesterol homeostasis |
| D | 0042986 | biological_process | positive regulation of amyloid precursor protein biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue OLA A 701 |
| Chain | Residue |
| A | PHE258 |
| A | ARG262 |
| A | MET265 |
| A | PHE392 |
| A | LEU428 |
| A | HIS460 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CLR A 702 |
| Chain | Residue |
| A | TRP186 |
| A | TRP189 |
| A | ILE190 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CLR A 703 |
| Chain | Residue |
| A | ARG272 |
| A | PRO276 |
| A | ASP435 |
| A | TRP438 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue CLR A 704 |
| Chain | Residue |
| A | ILE138 |
| A | ILE141 |
| A | TYR142 |
| A | PHE145 |
| A | ILE146 |
| A | CYS333 |
| A | TYR336 |
| A | PHE378 |
| A | PHE382 |
| A | TRP408 |
| B | HIS137 |
| B | THR140 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue ROV A 705 |
| Chain | Residue |
| A | THR380 |
| A | TYR416 |
| A | TRP420 |
| A | ASN421 |
| A | VAL424 |
| A | HIS460 |
| A | COA706 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue COA A 706 |
| Chain | Residue |
| A | TYR417 |
| A | ARG418 |
| A | HIS425 |
| A | TYR433 |
| A | LYS445 |
| A | MET449 |
| A | VAL452 |
| A | PHE453 |
| A | SER456 |
| A | PHE479 |
| A | ASP492 |
| A | ROV705 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | binding site for residue OLA B 701 |
| Chain | Residue |
| B | PHE258 |
| B | ILE261 |
| B | ARG262 |
| B | MET265 |
| B | PHE302 |
| B | LEU389 |
| B | VAL424 |
| B | LEU428 |
| B | SER456 |
| B | HIS460 |
| B | ROV705 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | binding site for residue 3VV B 702 |
| Chain | Residue |
| B | TYR413 |
| B | TYR417 |
| B | ARG418 |
| B | HIS425 |
| B | TYR433 |
| B | MET449 |
| B | VAL452 |
| B | PHE453 |
| B | SER456 |
| B | PHE479 |
| B | PHE486 |
| B | ASP492 |
| B | SER506 |
| B | GLY510 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue CLR B 703 |
| Chain | Residue |
| A | HIS137 |
| A | THR140 |
| B | ILE141 |
| B | TYR142 |
| B | ILE146 |
| B | LEU149 |
| B | GLY332 |
| B | CYS333 |
| B | PHE378 |
| B | PHE382 |
| B | TRP408 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue CLR B 704 |
| Chain | Residue |
| B | MET228 |
| B | VAL271 |
| B | PRO276 |
| B | TRP438 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue ROV B 705 |
| Chain | Residue |
| B | TRP420 |
| B | ASN421 |
| B | SER456 |
| B | HIS460 |
| B | OLA701 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue OLA C 701 |
| Chain | Residue |
| C | PHE258 |
| C | ARG262 |
| C | MET265 |
| C | PHE392 |
| C | LEU428 |
| C | HIS460 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue CLR C 702 |
| Chain | Residue |
| C | TRP186 |
| C | TRP189 |
| C | ILE190 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue CLR C 703 |
| Chain | Residue |
| C | PRO276 |
| C | ASP435 |
| C | TRP438 |
| C | ARG272 |
| site_id | AD6 |
| Number of Residues | 11 |
| Details | binding site for residue CLR C 704 |
| Chain | Residue |
| C | ILE141 |
| C | TYR142 |
| C | PHE145 |
| C | ILE146 |
| C | CYS333 |
| C | TYR336 |
| C | PHE378 |
| C | PHE382 |
| C | TRP408 |
| D | HIS137 |
| D | THR140 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for residue ROV C 705 |
| Chain | Residue |
| C | THR380 |
| C | TYR416 |
| C | TRP420 |
| C | ASN421 |
| C | VAL424 |
| C | HIS460 |
| C | COA706 |
| site_id | AD8 |
| Number of Residues | 12 |
| Details | binding site for residue COA C 706 |
| Chain | Residue |
| C | TYR417 |
| C | ARG418 |
| C | HIS425 |
| C | TYR433 |
| C | LYS445 |
| C | MET449 |
| C | VAL452 |
| C | PHE453 |
| C | SER456 |
| C | PHE479 |
| C | ASP492 |
| C | ROV705 |
| site_id | AD9 |
| Number of Residues | 11 |
| Details | binding site for residue OLA D 701 |
| Chain | Residue |
| D | PHE258 |
| D | ILE261 |
| D | ARG262 |
| D | MET265 |
| D | PHE302 |
| D | LEU389 |
| D | VAL424 |
| D | LEU428 |
| D | SER456 |
| D | HIS460 |
| D | ROV705 |
| site_id | AE1 |
| Number of Residues | 14 |
| Details | binding site for residue 3VV D 702 |
| Chain | Residue |
| D | TYR413 |
| D | TYR417 |
| D | ARG418 |
| D | HIS425 |
| D | TYR433 |
| D | MET449 |
| D | VAL452 |
| D | PHE453 |
| D | SER456 |
| D | PHE479 |
| D | PHE486 |
| D | ASP492 |
| D | SER506 |
| D | GLY510 |
| site_id | AE2 |
| Number of Residues | 11 |
| Details | binding site for residue CLR D 703 |
| Chain | Residue |
| C | HIS137 |
| C | THR140 |
| D | ILE141 |
| D | TYR142 |
| D | ILE146 |
| D | LEU149 |
| D | GLY332 |
| D | CYS333 |
| D | PHE378 |
| D | PHE382 |
| D | TRP408 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue CLR D 704 |
| Chain | Residue |
| D | MET228 |
| D | VAL271 |
| D | PRO276 |
| D | TRP438 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue ROV D 705 |
| Chain | Residue |
| D | TRP420 |
| D | ASN421 |
| D | SER456 |
| D | HIS460 |
| D | OLA701 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 968 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
| Chain | Residue | Details |
| A | MET1-ILE138 | |
| B | ASN491-LYS496 | |
| C | MET1-ILE138 | |
| C | ALA207-ILE218 | |
| C | ARG277-ARG319 | |
| C | LEU396-ARG443 | |
| C | ASN491-LYS496 | |
| D | MET1-ILE138 | |
| D | ALA207-ILE218 | |
| D | ARG277-ARG319 | |
| D | LEU396-ARG443 | |
| A | ALA207-ILE218 | |
| D | ASN491-LYS496 | |
| A | ARG277-ARG319 | |
| A | LEU396-ARG443 | |
| A | ASN491-LYS496 | |
| B | MET1-ILE138 | |
| B | ALA207-ILE218 | |
| B | ARG277-ARG319 | |
| B | LEU396-ARG443 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 84 |
| 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 | |
| C | ARG139-ASP160 | |
| D | ARG139-ASP160 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 272 |
| Details | TOPO_DOM: Lumenal => ECO:0000305 |
| Chain | Residue | Details |
| A | TYR161-LYS180 | |
| B | PRO529-PHE550 | |
| C | TYR161-LYS180 | |
| C | ALA245-SER252 | |
| C | LYS353-SER369 | |
| C | SER469-VAL474 | |
| C | PRO529-PHE550 | |
| D | TYR161-LYS180 | |
| D | ALA245-SER252 | |
| D | LYS353-SER369 | |
| D | SER469-VAL474 | |
| A | ALA245-SER252 | |
| D | PRO529-PHE550 | |
| A | LYS353-SER369 | |
| A | SER469-VAL474 | |
| A | PRO529-PHE550 | |
| B | TYR161-LYS180 | |
| B | ALA245-SER252 | |
| B | LYS353-SER369 | |
| B | SER469-VAL474 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 100 |
| 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 | |
| C | PHE181-TRP206 | |
| D | PHE181-TRP206 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 100 |
| 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 | |
| C | ARG219-LEU244 | |
| D | ARG219-LEU244 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 92 |
| 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 | |
| C | ARG253-PRO276 | |
| D | ARG253-PRO276 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 128 |
| 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 | |
| C | TRP320-ILE352 | |
| D | TRP320-ILE352 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 100 |
| 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 | |
| C | ILE370-MET395 | |
| D | ILE370-MET395 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 96 |
| 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 | |
| C | PHE444-LEU468 | |
| D | PHE444-LEU468 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 60 |
| 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 | |
| C | LEU475-VAL490 | |
| D | LEU475-VAL490 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 124 |
| 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 | |
| C | PRO497-CYS528 | |
| D | PRO497-CYS528 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| 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 | |
| C | HIS460 | |
| D | HIS460 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:32433613, ECO:0007744|PDB:6VUM |
| Chain | Residue | Details |
| A | HIS137 | |
| C | ARG418 | |
| C | TYR433 | |
| C | SER456 | |
| D | HIS137 | |
| D | ARG418 | |
| D | TYR433 | |
| D | SER456 | |
| A | ARG418 | |
| A | TYR433 | |
| A | SER456 | |
| B | HIS137 | |
| B | ARG418 | |
| B | TYR433 | |
| B | SER456 | |
| C | HIS137 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:32433614, ECO:0007744|PDB:6P2P |
| Chain | Residue | Details |
| A | ASN415 | |
| B | ASN415 | |
| C | ASN415 | |
| D | ASN415 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:32433614, ECO:0007744|PDB:6P2J |
| Chain | Residue | Details |
| A | ASN421 | |
| B | ASN421 | |
| C | ASN421 | |
| D | ASN421 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 8 |
| 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 | |
| C | HIS425 | |
| C | LYS445 | |
| D | HIS425 | |
| D | LYS445 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | MET1 | |
| B | MET1 | |
| C | MET1 | |
| D | MET1 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER8 | |
| B | SER8 | |
| C | SER8 | |
| D | SER8 |
