Cryo-EM structure of human diacylglycerol O-acyltransferase 1 complexed with acyl-CoA substrate

Structure

electron microscopy · 1 distinct chain.

Ligands and binding sites

• 6OU · [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate · ligand · 4 copies · chains A, B
• 3VV · S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3, 5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2, 4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (9Z)-octadec-9-enethioate (non-preferred name) · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

• 6VZ1 · Cryo-EM structure of human diacylglycerol O-acyltransferase 1 complexed with acyl-CoA… · the same entry in another collection · chain A against A, TM-score 1.00
• O75907 · AlphaFold monomer V2.0 prediction for diacylglycerol O-acyltransferase 1 (O75907) · a predicted model of the same protein · chain A against A, TM-score 0.83

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt O75907
• Elsewhere: RCSB PDB 6VZ1 · PDBe 6VZ1 · UniProt O75907