PDBe 1q12

X-ray diffraction
2.6Å resolution

Crystal Structure of the ATP-bound E. coli MalK

Released:

Function and Biology Details

Reaction catalysed:
ATP + H(2)O + maltose-[maltose-binding protein](Side 1) = ADP + phosphate + maltose(Side 2) + [maltose-binding protein](Side 1)
Biochemical function:
Biological process:

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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P1
Unit cell:
a: 59.88Å b: 97.278Å c: 101.862Å
α: 74.59° β: 82.47° γ: 76.85°
R-values:
R R work R free
0.258 0.258 0.286
Expression system: Escherichia coli