› 2nqt

X-ray diffraction
1.58Å resolution

Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis at 1.58 A resolution

Released:
DOI: 10.2210/pdb2nqt/pdb
PDB entry 2nqt coloured by chain, front view.
PDB entry 2nqt coloured by chain, side view.
PDB entry 2nqt coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase from Mycobacterium tuberculosis in complex with NADP(+).
Cherney LT, Cherney MM, Garen CR, Niu C, Moradian F, James MN
J Mol Biol 367 1357-69 (2007)
PMID: 17316682

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:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-162036 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyl-gamma-glutamyl-phosphate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 352 amino acids
Theoretical weight: 36.37 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WPZ9 (Residues: 1-352; Coverage: 100%)
Gene names: MTCY06H11.17, Rv1652, argC
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand CSD 2 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 140.877Å b: 77.983Å c: 87.884Å
α: 90° β: 127.38° γ: 90°
R-values:
R R work R free
0.164 0.163 0.185
Expression system: Escherichia coli

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Citations

1 review citation

Structural genomics approach to drug discovery for Mycobacterium tuberculosis.
Ioerger et al. (2009)
6 other articles

2 mentions without citation

Structural preferences of cysteine sulfinic acid: The sulfinate engages in multiple local interactions with the peptide backbone.
Urmey et al. (2020)
1 more