5kp2

X-ray diffraction
2Å resolution

Beta-ketoacyl-ACP synthase III -2 (FabH2) (C113A) from Vibrio Cholerae cocrystallized with octanoyl-CoA: hydrolzed ligand

Released:
Entry authors: Hou J, Zheng H, Grabowski M, Anderson WF, Minor W, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO(2) 
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 362 amino acids
Theoretical weight: 39.04 KDa
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9KLJ3 (Residues: 1-359; Coverage: 99%)
Gene names: VC_A0751, fabH2
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments


Cofactor: Ligand COA 1 x COA
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21
Unit cell:
a: 84.67Å b: 61.242Å c: 71.524Å
α: 90° β: 94.67° γ: 90°
R-values:
R R work R free
0.195 0.194 0.221
Expression system: Escherichia coli BL21