› 6c0v

Electron Microscopy
3.4Å resolution

Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation

Released:
DOI: 10.2210/pdb6c0v/pdb
PDB entry 6c0v coloured by chain, front view.
PDB entry 6c0v coloured by chain, side view.
PDB entry 6c0v coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation.
Kim Y, Chen J
Science 359 915-919 (2018)
PMID: 29371429
Related structures: EMD-7325

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139987 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent translocase ABCB1 Chain: A
Molecule details ›
Chain: A
Length: 1289 amino acids
Theoretical weight: 142.66 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P08183 (Residues: 1-1280; Coverage: 100%)
Gene names: ABCB1, MDR1, PGY1
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand ATP 2 x ATP
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.4Å
Relevant EMDB volumes: EMD-7325
Expression system: Homo sapiens

Quick links

Citations

33 review citations

Emerging Diversity in Lipid-Protein Interactions.
Corradi et al. (2019)
32 more

75 mentions without citation

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