5xi0

X-ray diffraction
2.09Å resolution

Crystal structure of FabV, a new class of enyl-acyl carrier protein reductase from Vibrio fischeri

Released:
Source organism: Aliivibrio fischeri ES114
Entry author: Park AK

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:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-177001 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] Chains: A, B
Molecule details ›
Chains: A, B
Length: 400 amino acids
Theoretical weight: 43.82 KDa
Source organism: Aliivibrio fischeri ES114
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5E6G3 (Residues: 1-400; Coverage: 100%)
Gene names: VF_0888, fabV
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Unit cell:
a: 62.998Å b: 109.175Å c: 119.831Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.206 0.272
Expression system: Escherichia coli