6VZ1
Cryo-EM structure of human diacylglycerol O-acyltransferase 1 complexed with acyl-CoA substrate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003846 | molecular_function | 2-acylglycerol O-acyltransferase activity |
| A | 0004144 | molecular_function | diacylglycerol O-acyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006640 | biological_process | monoacylglycerol biosynthetic process |
| A | 0006641 | biological_process | triglyceride metabolic process |
| A | 0008374 | molecular_function | O-acyltransferase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0019432 | biological_process | triglyceride biosynthetic process |
| A | 0019915 | biological_process | lipid storage |
| A | 0034379 | biological_process | very-low-density lipoprotein particle assembly |
| A | 0035336 | biological_process | long-chain fatty-acyl-CoA metabolic process |
| A | 0035579 | cellular_component | specific granule membrane |
| A | 0042572 | biological_process | retinol metabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0046339 | biological_process | diacylglycerol metabolic process |
| A | 0046486 | biological_process | glycerolipid metabolic process |
| A | 0050252 | molecular_function | retinol O-fatty-acyltransferase activity |
| A | 0055089 | biological_process | fatty acid homeostasis |
| B | 0003846 | molecular_function | 2-acylglycerol O-acyltransferase activity |
| B | 0004144 | molecular_function | diacylglycerol O-acyltransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006640 | biological_process | monoacylglycerol biosynthetic process |
| B | 0006641 | biological_process | triglyceride metabolic process |
| B | 0008374 | molecular_function | O-acyltransferase activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0019432 | biological_process | triglyceride biosynthetic process |
| B | 0019915 | biological_process | lipid storage |
| B | 0034379 | biological_process | very-low-density lipoprotein particle assembly |
| B | 0035336 | biological_process | long-chain fatty-acyl-CoA metabolic process |
| B | 0035579 | cellular_component | specific granule membrane |
| B | 0042572 | biological_process | retinol metabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| B | 0046339 | biological_process | diacylglycerol metabolic process |
| B | 0046486 | biological_process | glycerolipid metabolic process |
| B | 0050252 | molecular_function | retinol O-fatty-acyltransferase activity |
| B | 0055089 | biological_process | fatty acid homeostasis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue 6OU A 501 |
| Chain | Residue |
| A | SER78 |
| B | TYR339 |
| B | 6OU502 |
| A | TYR452 |
| A | ALA455 |
| B | ARG86 |
| B | ALA101 |
| B | PHE104 |
| B | ARG280 |
| B | ARG281 |
| B | PHE287 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue 6OU A 502 |
| Chain | Residue |
| A | ARG86 |
| A | LEU89 |
| A | CYS92 |
| A | VAL93 |
| A | SER99 |
| A | ASN100 |
| A | PHE288 |
| A | LEU291 |
| A | LEU335 |
| A | ILE336 |
| A | PHE338 |
| A | TYR339 |
| A | TRP364 |
| B | ILE88 |
| B | TRP91 |
| B | 6OU501 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue 3VV A 503 |
| Chain | Residue |
| A | TRP374 |
| A | GLN375 |
| A | VAL381 |
| A | HIS382 |
| A | ILE386 |
| A | TYR390 |
| A | ARG404 |
| A | SER411 |
| A | HIS415 |
| A | VAL469 |
| A | TYR476 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue 6OU B 501 |
| Chain | Residue |
| A | ARG86 |
| A | VAL93 |
| A | PHE104 |
| A | LEU105 |
| A | ARG280 |
| A | ARG281 |
| A | GLU284 |
| A | TYR339 |
| A | 6OU502 |
| B | PHE76 |
| B | SER78 |
| B | ASN451 |
| B | TYR452 |
| B | ALA455 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | binding site for residue 6OU B 502 |
| Chain | Residue |
| A | PHE76 |
| A | ILE88 |
| A | TRP91 |
| A | 6OU501 |
| B | LEU89 |
| B | CYS92 |
| B | VAL93 |
| B | MET95 |
| B | LEU96 |
| B | SER99 |
| B | PHE288 |
| B | LEU291 |
| B | LEU295 |
| B | TYR339 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue 3VV B 503 |
| Chain | Residue |
| B | TRP374 |
| B | GLN375 |
| B | HIS382 |
| B | ILE386 |
| B | TYR390 |
| B | LYS391 |
| B | ARG404 |
| B | SER411 |
| B | HIS415 |
| B | LEU423 |
| B | TYR476 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 362 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611 |
| Chain | Residue | Details |
| A | MET1-SER83 | |
| A | GLY157-GLU161 | |
| A | LYS224-ILE273 | |
| A | GLN354-SER399 | |
| A | PHE448-GLN449 | |
| B | MET1-SER83 | |
| B | GLY157-GLU161 | |
| B | LYS224-ILE273 | |
| B | GLN354-SER399 | |
| B | PHE448-GLN449 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 68 |
| Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0, ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1 |
| Chain | Residue | Details |
| A | ASN84-ILE118 | |
| B | ASN84-ILE118 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 72 |
| Details | TOPO_DOM: Lumenal => ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611 |
| Chain | Residue | Details |
| A | GLN119-SER130 | |
| A | LEU185-PRO191 | |
| A | LYS309-ASP315 | |
| A | VAL421-LEU428 | |
| A | GLU482-ALA488 | |
| B | GLN119-SER130 | |
| B | LEU185-PRO191 | |
| B | LYS309-ASP315 | |
| B | VAL421-LEU428 | |
| B | GLU482-ALA488 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 50 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0, ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1 |
| Chain | Residue | Details |
| A | TRP131-VAL156 | |
| B | TRP131-VAL156 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 44 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0, ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1 |
| Chain | Residue | Details |
| A | GLN162-LEU184 | |
| B | GLN162-LEU184 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 62 |
| Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0, ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1 |
| Chain | Residue | Details |
| A | VAL192-ALA223 | |
| B | VAL192-ALA223 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 68 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0, ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1 |
| Chain | Residue | Details |
| A | ARG274-MET308 | |
| B | ARG274-MET308 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 74 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0, ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1 |
| Chain | Residue | Details |
| A | TYR316-MET353 | |
| B | TYR316-MET353 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0, ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1 |
| Chain | Residue | Details |
| A | LYS400-SER420 | |
| B | LYS400-SER420 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 36 |
| Details | TRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0, ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1 |
| Chain | Residue | Details |
| A | TRP429-PHE447 | |
| B | TRP429-PHE447 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 62 |
| Details | TRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0, ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1 |
| Chain | Residue | Details |
| A | GLY450-TYR481 | |
| B | GLY450-TYR481 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:32433610 |
| Chain | Residue | Details |
| A | HIS415 | |
| B | HIS415 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0, ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1 |
| Chain | Residue | Details |
| B | TRP374 | |
| B | TYR390 | |
| A | TRP374 | |
| A | TYR390 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:32433610, ECO:0007744|PDB:6VP0 |
| Chain | Residue | Details |
| A | ARG404 | |
| B | ARG404 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1 |
| Chain | Residue | Details |
| A | TYR477 | |
| B | TYR477 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | SITE: Important for catalytic activity => ECO:0000269|PubMed:32433610 |
| Chain | Residue | Details |
| A | GLU416 | |
| B | GLU416 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER17 | |
| A | SER18 | |
| B | SER17 | |
| B | SER18 |
