› 6ah9

X-ray diffraction
1.74Å resolution

Crystal structure of enoyl-ACP reductase from Acinetobacter baumannii in complex with NAD and Triclosan

Released:
DOI: 10.2210/pdb6ah9/pdb
PDB entry 6ah9 coloured by chain, front view.
PDB entry 6ah9 coloured by chain, side view.
PDB entry 6ah9 coloured by chain, top view.
Source organism: Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841
Entry authors: Rani ST, Nataraj V, Laxminarasimhan A, Thomas A, Krishnamurthy N

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111933 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] Chain: A
Molecule details ›
Chain: A
Length: 267 amino acids
Theoretical weight: 28.66 KDa
Source organism: Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D0CAD5 (Residues: 22-288; Coverage: 93%)
Gene names: HMPREF0010_01715, fabI
Sequence domains: Enoyl-(Acyl carrier protein) reductase

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
1 bound ligand:
Ligand TCL 1 x TCL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: I222
Unit cell:
a: 77.212Å b: 77.245Å c: 85.207Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.195 0.241
Expression system: Escherichia coli BL21(DE3)

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