› 5i9n

X-ray diffraction
2.51Å resolution

Crystal structure of B. pseudomallei FabI in complex with NAD and PT412

Released:
DOI: 10.2210/pdb5i9n/pdb
PDB entry 5i9n coloured by chain, front view.
PDB entry 5i9n coloured by chain, side view.
PDB entry 5i9n coloured by chain, top view.
Source organism: Burkholderia pseudomallei
Primary publication:
Rationalizing the Binding Kinetics for the Inhibition of the Burkholderia pseudomallei FabI1 Enoyl-ACP Reductase.
Neckles C, Eltschkner S, Cummings JE, Hirschbeck M, Daryaee F, Bommineni GR, Zhang Z, Spagnuolo L, Yu W, Davoodi S, Slayden RA, Kisker C, Tonge PJ
Biochemistry 56 1865-1878 (2017)
PMID: 28225601

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
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101892 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] Chain: A
Molecule details ›
Chain: A
Length: 276 amino acids
Theoretical weight: 29.33 KDa
Source organism: Burkholderia pseudomallei
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H3HP34 (Residues: 1-263; Coverage: 100%)
Gene names: BP1026B_I1187, fabI
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
1 bound ligand:
Ligand 69J 1 x 69J
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: I222
Unit cell:
a: 72.63Å b: 74.67Å c: 96.75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.156 0.215
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structural approaches to pathway-specific antimicrobial agents.
Johnson et al. (2020)
2 other articles

1 mention without citation

Rationalizing the Binding Kinetics for the Inhibition of the Burkholderia pseudomallei FabI1 Enoyl-ACP Reductase.
Neckles et al. (2017)