› 1vkn

X-ray diffraction
1.8Å resolution

Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (TM1782) from Thermotoga maritima at 1.80 A resolution

Released:
DOI: 10.2210/pdb1vkn/pdb
PDB entry 1vkn coloured by chain, front view.
PDB entry 1vkn coloured by chain, side view.
PDB entry 1vkn coloured by chain, top view.
Source organism: Thermotoga maritima
Entry author: Joint Center for Structural Genomics (JCSG)

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 domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194884 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyl-gamma-glutamyl-phosphate reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 351 amino acids
Theoretical weight: 39.87 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X2A2 (Residues: 1-339; Coverage: 100%)
Gene names: TM_1782, argC
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 36 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P21
Unit cell:
a: 85.098Å b: 92.103Å c: 100.88Å
α: 90° β: 112.76° γ: 90°
R-values:
R R work R free
0.179 0.178 0.212
Expression system: Escherichia coli

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