› 4efi

X-ray diffraction
1.35Å resolution

Function and Biology Details

Reaction catalysed: 
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-171880 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-(Acyl-carrier protein) synthase Chain: A
Molecule details ›
Chain: A
Length: 354 amino acids
Theoretical weight: 37.86 KDa
Source organism: Paraburkholderia xenovorans LB400
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13SV4 (Residues: 1-354; Coverage: 100%)
Gene name: Bxe_A0096
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

3 bound ligands:
Ligand UNL 1 x UNL
Ligand CL 1 x CL
Ligand FMT 1 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: C2
Unit cell:
a: 101.377Å b: 54.408Å c: 60.836Å
α: 90° β: 103.77° γ: 90°
R-values:
R R work R free
0.16 0.159 0.174
Expression system: Escherichia coli BL21(DE3)

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