› 6p2j

Electron Microscopy
3Å resolution

Dimeric structure of ACAT1

Released:
DOI: 10.2210/pdb6p2j/pdb
PDB entry 6p2j coloured by chain, front view.
PDB entry 6p2j coloured by chain, side view.
PDB entry 6p2j coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for catalysis and substrate specificity of human ACAT1.
Qian H, Zhao X, Yan R, Yao X, Gao S, Sun X, Du X, Yang H, Wong CCL, Yan N
Nature 581 333-338 (2020)
PMID: 32433614
Related structures: EMD-20238

Function and Biology Details

Reaction catalysed: 
A long-chain acyl-CoA + a sterol = CoA + a long-chain 3-hydroxysterol ester
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152963 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sterol O-acyltransferase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 594 amino acids
Theoretical weight: 69.75 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P35610 (Residues: 1-550; Coverage: 100%)
Gene names: ACACT, ACACT1, ACAT, ACAT1, SOAT, SOAT1, STAT
Sequence domains: MBOAT, membrane-bound O-acyltransferase family

Ligands and Environments

1 bound ligand:
Ligand 3VV 2 x 3VV
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3Å
Relevant EMDB volumes: EMD-20238
Expression system: Homo sapiens

Quick links

Citations

11 review citations

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

2 mentions without citation

A rising tide lifts all MBOATs: recent progress in structural and functional understanding of membrane bound O-acyltransferases.
Pierce et al. (2023)
1 more