› 4eg0

X-ray diffraction
1.65Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109466 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-alanine--D-alanine ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 317 amino acids
Theoretical weight: 33.73 KDa
Source organism: Burkholderia ambifaria MC40-6
Expression system: Escherichia coli
UniProt:
  • Canonical: B1YSS6 (Residues: 1-313; Coverage: 100%)
Gene names: BamMC406_0490, ddl
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand EDO 5 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P21
Unit cell:
a: 48.38Å b: 118.11Å c: 56.93Å
α: 90° β: 91.56° γ: 90°
R-values:
R R work R free
0.175 0.173 0.2
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.
Dailey et al. (2017)
10 more

2 mentions without citation

Combining functional and structural genomics to sample the essential Burkholderia structome.
Baugh et al. (2013)
1 more