X-ray diffraction
2Å resolution

Crystal structure of Enoyl-[acyl-carrier-protein] reductase (NADH) from Aquifex aeolicus VF5

Source organism: Aquifex aeolicus VF5
Entry authors: Chen L, Li Y, Ebihara A, Shinkai A, Kuramitsu S, Yokoyama S, Zhao M, Rose JP, Wang B-C, Southeast Collaboratory for Structural Genomics (SECSG), RIKEN Structural Genomics/Proteomics Initiative (RSGI)

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)
Entry contents:
1 distinct polypeptide molecule
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 285 amino acids
Theoretical weight: 31.54 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
  • Canonical: O67505 (Residues: 1-270; Coverage: 100%)
Gene names: aq_1552, fabI
Sequence domains: Enoyl-(Acyl carrier protein) reductase
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: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 72.078Å b: 119.019Å c: 119.197Å
α: 90° β: 90° γ: 90°
R R work R free
0.169 0.167 0.197
Expression system: Escherichia coli