PDBe 2awo

X-ray diffraction
2.8Å resolution

Crystal structure of the ADP-Mg-bound E. Coli MALK (Crystallized with ADP-Mg)

Released:
Source organism: Escherichia coli K-12
Primary publication:
ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation.
Proc. Natl. Acad. Sci. U.S.A. 102 17969-74 (2005)
PMID: 16326809

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Maltose/maltodextrin import ATP-binding protein MalK Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 381 amino acids
Theoretical weight: 42.18 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P68187 (Residues: 1-371; Coverage: 100%)
Gene names: JW3995, b4035, malK
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21
Unit cell:
a: 70.213Å b: 101.975Å c: 131.503Å
α: 90° β: 90.73° γ: 90°
R-values:
R R work R free
0.239 0.239 0.277
Expression system: Escherichia coli