3s8m

X-ray diffraction
1.6Å resolution

The Crystal Structure of FabV

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] Chain: A
Molecule details ›
Chain: A
Length: 422 amino acids
Theoretical weight: 46.25 KDa
Source organism: Xanthomonas oryzae pv. oryzae MAFF 311018
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q2P9J6 (Residues: 1-402; Coverage: 100%)
Gene names: XOO0026, fabV
Sequence domains:
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: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 50.52Å b: 74.53Å c: 107.39Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.185 0.205
Expression system: Escherichia coli BL21(DE3)