X-ray diffraction
1.8Å resolution

Crystal structure of Chlamydia trachomatis enoyl-ACP reductase (FabI) in complex with NADH and AFN-1252


Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Enoyl-[acyl-carrier-protein] reductase [NADH] Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 298 amino acids
Theoretical weight: 31.99 KDa
Source organism: Chlamydia trachomatis F/11-96
Expression system: Escherichia coli BL21(DE3)
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P43
Unit cell:
a: 96.146Å b: 96.146Å c: 263.082Å
α: 90° β: 90° γ: 90°
R R work R free
0.188 0.186 0.229
Expression system: Escherichia coli BL21(DE3)