X-ray diffraction
1.85Å resolution

Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis in complex with NADP+.


Function and Biology Details

Reaction catalysed:
N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = N-acetyl-L-glutamyl 5-phosphate + NADPH
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
N-acetyl-gamma-glutamyl-phosphate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 352 amino acids
Theoretical weight: 36.34 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
  • Canonical: P9WPZ9 (Residues: 1-352; Coverage: 100%)
Gene names: MTCY06H11.17, Rv1652, argC
Sequence domains:
Structure domains:

Ligands and Environments

Cofactor: Ligand NAP 2 x NAP
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 141.456Å b: 78.214Å c: 88.034Å
α: 90° β: 127.46° γ: 90°
R R work R free
0.163 0.161 0.205
Expression system: Escherichia coli