4eit

X-ray diffraction
2.4Å resolution

Crystal structure of an enoyl-(acyl carrier protein) reductase from Bartonella henselae

Released:
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed:
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-102130 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 276 amino acids
Theoretical weight: 30.08 KDa
Source organism: Bartonella henselae str. Houston-1
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H3M2Q2 (Residues: 1-272; Coverage: 100%)
Gene names: BH04310, fabI2
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: C2
Unit cell:
a: 122.36Å b: 76.86Å c: 171.95Å
α: 90° β: 107.99° γ: 90°
R-values:
R R work R free
0.197 0.196 0.226
Expression system: Escherichia coli