4iql

X-ray diffraction
1.94Å resolution

Crystal Structure of Porphyromonas gingivalis Enoyl-ACP Reductase II (FabK) with cofactors NADPH and FMN

Released:
Source organism: Porphyromonas gingivalis W83
Primary publication:
Structural characterization of Porphyromonas gingivalis enoyl-ACP reductase II (FabK).
Acta Crystallogr F Struct Biol Commun 74 105-112 (2018)
PMID: 29400320

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:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-181715 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nitronate monooxygenase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 333 amino acids
Theoretical weight: 35.32 KDa
Source organism: Porphyromonas gingivalis W83
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7MAW0 (Residues: 1-313; Coverage: 100%)
Gene names: PG_1416, fabK
Sequence domains: Nitronate monooxygenase
Structure domains: Aldolase class I

Ligands and Environments


Cofactor: Ligand NDP 4 x NDP

Cofactor: Ligand FMN 2 x FMN
2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 48.652Å b: 86.652Å c: 150.505Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.161 0.207
Expression system: Escherichia coli BL21(DE3)