› 5ugs

X-ray diffraction
2.8Å 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, E, G
Molecule details ›
Chains: A, B, C, D, E, G
Length: 289 amino acids
Theoretical weight: 30.73 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
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 6 x NAD
3 bound ligands:
Ligand XT5 7 x XT5
Ligand CL 10 x CL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Unit cell:
a: 91.92Å b: 130.359Å c: 176.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.244
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Binding kinetics of ligands acting at GPCRs.
Sykes et al. (2019)
3 more

1 mention without citation

Binding Thermodynamics and Dissociation Kinetics Analysis Uncover the Key Structural Motifs of Phenoxyphenol Derivatives as the Direct InhA Inhibitors and the Hotspot Residues of InhA.
Zhang et al. (2022)