X-ray diffraction
1.78Å resolution

Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Vibrio Cholerae in complex with Coenzyme A

Entry authors: Hou J, Zheng H, Langner K, 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
3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 319 amino acids
Theoretical weight: 34.1 KDa
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q9KQH5 (Residues: 1-316; Coverage: 100%)
Gene names: VC_2023, fabH1
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

Cofactor: Ligand COA 4 x COA
2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P212121
Unit cell:
a: 99.449Å b: 100.248Å c: 132.763Å
α: 90° β: 90° γ: 90°
R R work R free
0.172 0.17 0.196
Expression system: Escherichia coli BL21(DE3)