X-ray diffraction
1.7Å resolution

Crystal Structure of a Possible Enoyl-(acyl-carrier-protein) Reductase from Brucella melitensis

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 dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Enoyl-[acyl-carrier-protein] reductase [NADH] Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 293 amino acids
Theoretical weight: 31.62 KDa
Source organism: Brucella abortus bv. 1 str. 9-941
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q57A95 (Residues: 1-272; Coverage: 100%)
Gene names: BruAb1_2144, fabI-2
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

Cofactor: Ligand NAD 8 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P1
Unit cell:
a: 64.91Å b: 83.83Å c: 106.29Å
α: 90.25° β: 100.08° γ: 90.82°
R R work R free
0.148 0.146 0.176
Expression system: Escherichia coli BL21(DE3)