4m87

X-ray diffraction
2.25Å resolution

Crystal Structure of Enoyl-Acyl Carrier Protein Reductase (FabI) from Neisseria meningitidis in complex with NAD+

Released:
Source organism: Neisseria meningitidis FAM18
Entry authors: Nanson JD, Forwood JK

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)
PDBe Complex ID:
PDB-CPX-106651 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] Chains: A, B
Molecule details ›
Chains: A, B
Length: 261 amino acids
Theoretical weight: 27.72 KDa
Source organism: Neisseria meningitidis FAM18
Expression system: Escherichia coli
UniProt:
  • Canonical: A1KVU8 (Residues: 1-261; Coverage: 100%)
Gene names: NMC1834, fabI
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P6122
Unit cell:
a: 91.1Å b: 91.1Å c: 240.84Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 0.169 0.189
Expression system: Escherichia coli