› 5zxd

X-ray diffraction
2.29Å resolution

Crystal structure of ATP-bound human ABCF1

Released:
DOI: 10.2210/pdb5zxd/pdb
PDB entry 5zxd coloured by chain, front view.
PDB entry 5zxd coloured by chain, side view.
PDB entry 5zxd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal Structure of ATP-Bound Human ABCF1 Demonstrates a Unique Conformation of ABC Proteins.
Qu L, Jiang Y, Cheng C, Wu D, Meng B, Chen Z, Zhu Y, Shaw N, Ouyang S, Liu ZJ
Structure 26 1259-1265.e3 (2018)
PMID: 30017566

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185505 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-binding cassette sub-family F member 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 546 amino acids
Theoretical weight: 62.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: Q8NE71 (Residues: 300-841; Coverage: 64%)
Gene names: ABC50, ABCF1
Sequence domains: ABC transporter

Ligands and Environments

1 bound ligand:
Ligand ATP 4 x ATP
1 modified residue:
Ligand MSE 20 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U1
Spacegroup: P212121
Unit cell:
a: 66.068Å b: 132.814Å c: 148.329Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.194 0.224
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

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Citations

7 citation in other articles

A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling.
Kasari et al. (2019)
6 more

1 mention without citation

ABC-F translation factors: from antibiotic resistance to immune response.
Fostier et al. (2021)