› 4myc

X-ray diffraction
3.06Å resolution

Structure of the mitochondrial ABC transporter, Atm1

Released:
DOI: 10.2210/pdb4myc/pdb
PDB entry 4myc coloured by chain, front view.
PDB entry 4myc coloured by chain, side view.
PDB entry 4myc coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1.
Srinivasan V, Pierik AJ, Lill R
Science 343 1137-40 (2014)
PMID: 24604199

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154114 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Iron-sulfur clusters transporter ATM1, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 598 amino acids
Theoretical weight: 67.21 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P40416 (Residues: 98-690; Coverage: 86%)
Gene names: ATM1, MDY, YM9952.03C, YMR301C
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P6522
Unit cell:
a: 156.618Å b: 156.618Å c: 520.562Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.253 0.251 0.298
Expression system: Escherichia coli

Quick links

Citations

38 review citations

Mechanistic diversity in ATP-binding cassette (ABC) transporters.
Locher KP. (2016)
37 more

17 mentions without citation

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