› 5xjy

Electron Microscopy
4.1Å resolution

Cryo-EM structure of human ABCA1

Released:
DOI: 10.2210/pdb5xjy/pdb
PDB entry 5xjy coloured by chain, front view.
PDB entry 5xjy coloured by chain, side view.
PDB entry 5xjy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the Human Lipid Exporter ABCA1.
Qian H, Zhao X, Cao P, Lei J, Yan N, Gong X
Cell 169 1228-1239.e10 (2017)
PMID: 28602350
Related structures: EMD-6724

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131940 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Phospholipid-transporting ATPase ABCA1 Chain: A
Molecule details ›
Chain: A
Length: 2305 amino acids
Theoretical weight: 259.51 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O95477 (Residues: 1-2261; Coverage: 100%)
Gene names: ABC1, ABCA1, CERP
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand NAG 5 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4.1Å
Relevant EMDB volumes: EMD-6724
Expression system: Spodoptera frugiperda

Quick links

Citations

42 review citations

Comparison of mechanistic transport cycle models of ABC exporters.
Szöllősi et al. (2018)
41 more

35 mentions without citation

Structural and functional diversity calls for a new classification of ABC transporters.
Thomas et al. (2020)
34 more