X-ray diffraction
1.8Å resolution

Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH (MR, cleaved Histag)


Function and Biology Details

Reaction catalysed:
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
Enoyl-[acyl-carrier-protein] reductase [NADH] Chain: A
Molecule details ›
Chain: A
Length: 405 amino acids
Theoretical weight: 44.03 KDa
Source organism: Yersinia pestis CO92
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q8Z9U1 (Residues: 1-399; Coverage: 100%)
Gene names: YPO4104, YP_4011, fabV, y4119
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

Cofactor: Ligand NAI 1 x NAI
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P3121
Unit cell:
a: 102.16Å b: 102.16Å c: 84.761Å
α: 90° β: 90° γ: 120°
R R work R free
0.17 0.168 0.212
Expression system: Escherichia coli BL21(DE3)