› 3m1l

X-ray diffraction
2.52Å resolution

Crystal structure of a C-terminal trunacted mutant of a putative ketoacyl reductase (FabG4) from Mycobacterium tuberculosis H37Rv at 2.5 Angstrom resolution

Released:
DOI: 10.2210/pdb3m1l/pdb
PDB entry 3m1l coloured by chain, front view.
PDB entry 3m1l coloured by chain, side view.
PDB entry 3m1l coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Crystal structure of FabG4 from Mycobacterium tuberculosis reveals the importance of C-terminal residues in ketoreductase activity.
Dutta D, Bhattacharyya S, Mukherjee S, Saha B, Das AK
J Struct Biol 174 147-55 (2011)
PMID: 21081168

Function and Biology Details

Reaction catalysed: 
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129464 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-(Acyl-carrier-protein) reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 432 amino acids
Theoretical weight: 44.56 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: O53665 (Residues: 17-448; Coverage: 95%)
Gene names: MT0256, fabG-1
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

1 bound ligand:
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 65.076Å b: 80.497Å c: 153.953Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.241
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Crystal structure of hexanoyl-CoA bound to β-ketoacyl reductase FabG4 of Mycobacterium tuberculosis.
Dutta et al. (2013)
7 more

1 mention without citation

Insights into Acinetobacter baumannii fatty acid synthesis 3-oxoacyl-ACP reductases.
Cross et al. (2021)