Electron Microscopy
3.4Å resolution

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

Source organism: Homo sapiens
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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
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
  • Canonical: P08183 (Residues: 1-1280; Coverage: 100%)
Gene names: ABCB1, MDR1, PGY1
Sequence domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

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