4hzn

X-ray diffraction
2.25Å resolution

The Structure of the Bifunctional Acetyltransferase/Decarboxylase LnmK from the Leinamycin Biosynthetic Pathway Revealing Novel Activity for a Double Hot Dog Fold

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-184515 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
LnmK N-terminal domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 333 amino acids
Theoretical weight: 37.38 KDa
Source organism: Streptomyces atroolivaceus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8GGP1 (Residues: 1-319; Coverage: 100%)
Gene name: LnmK
Sequence domains: LnmK N-terminal Hot Dog Fold domain
Structure domains: Hotdog Thioesterase

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P6122
Unit cell:
a: 60.165Å b: 60.165Å c: 311.193Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.2 0.254
Expression system: Escherichia coli BL21(DE3)