› 6vp0

Electron Microscopy
3.1Å resolution

Human Diacylglycerol Acyltransferase 1 in complex with oleoyl-CoA

Released:
DOI: 10.2210/pdb6vp0/pdb
PDB entry 6vp0 coloured by chain, front view.
PDB entry 6vp0 coloured by chain, side view.
PDB entry 6vp0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and mechanism of human diacylglycerol O-acyltransferase 1.
Wang L, Qian H, Nian Y, Han Y, Ren Z, Zhang H, Hu L, Prasad BVV, Laganowsky A, Yan N, Zhou M
Nature 581 329-332 (2020)
PMID: 32433610
Related structures: EMD-21302

Function and Biology Details

Reactions catalysed: 
Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol
Acyl-CoA + retinol = CoA + retinyl ester
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131166 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Diacylglycerol O-acyltransferase 1 Chains: C, E
Molecule details ›
Chains: C, E
Length: 488 amino acids
Theoretical weight: 55.34 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: O75907 (Residues: 1-488; Coverage: 100%)
Gene names: AGRP1, DGAT, DGAT1
Sequence domains: MBOAT, membrane-bound O-acyltransferase family

Ligands and Environments

4 bound ligands:
Ligand POV 4 x POV
Ligand P5S 4 x P5S
Ligand 3VV 2 x 3VV
Ligand AV0 2 x AV0
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.1Å
Relevant EMDB volumes: EMD-21302
Expression system: Trichoplusia ni

Quick links

Citations

10 review citations

Hepatic lipid droplets: A balancing act between energy storage and metabolic dysfunction in NAFLD.
Mashek DG. (2021)
9 more

5 mentions without citation

Update and nomenclature proposal for mammalian lysophospholipid acyltransferases, which create membrane phospholipid diversity.
Valentine et al. (2022)
4 more