› 6vxi

Electron Microscopy
3.7Å resolution

Structure of ABCG2 bound to mitoxantrone

Released:
DOI: 10.2210/pdb6vxi/pdb
PDB entry 6vxi coloured by chain, front view.
PDB entry 6vxi coloured by chain, side view.
PDB entry 6vxi coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
ABCG2 transports anticancer drugs via a closed-to-open switch.
Orlando BJ, Liao M
OpenAccess logo Nat Commun 11 2264 (2020)
PMID: 32385283
Related structures: EMD-21438

Function and Biology Details

Reaction catalysed: 
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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194005 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Broad substrate specificity ATP-binding cassette transporter ABCG2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 655 amino acids
Theoretical weight: 72.39 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q9UNQ0 (Residues: 1-655; Coverage: 100%)
Gene names: ABCG2, ABCP, BCRP, BCRP1, MXR
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand CLR 2 x CLR
Ligand MIX 1 x MIX
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 3.7Å
Relevant EMDB volumes: EMD-21438
Expression system: Homo sapiens

Quick links

Citations

13 review citations

Clinically-Relevant ABC Transporter for Anti-Cancer Drug Resistance.
Xiao et al. (2021)
12 more

20 mentions without citation

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