› 5g0u

X-ray diffraction
1.73Å resolution

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161512 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 269 amino acids
Theoretical weight: 28.55 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WGR1 (Residues: 1-269; Coverage: 100%)
Gene names: MTCY277.05, Rv1484, inhA
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
1 bound ligand:
Ligand 9CV 2 x 9CV
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 65.467Å b: 114.117Å c: 68.482Å
α: 90° β: 97.62° γ: 90°
R-values:
R R work R free
0.184 0.182 0.217
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

DNA-encoded chemistry: enabling the deeper sampling of chemical space.
Goodnow et al. (2017)
4 more

2 mentions without citation

Discovery of cofactor-specific, bactericidal Mycobacterium tuberculosis InhA inhibitors using DNA-encoded library technology.
Soutter et al. (2016)
1 more