2ozp

X-ray diffraction
2.01Å resolution

Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (TTHA1904) from Thermus thermophilus

Released:
Source organism: Thermus thermophilus HB8
Entry authors: Rehse PH, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed:
An [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + phosphate + NADP(+) = an [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-glutamine + NADPH
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
PDBe Complex ID:
PDB-CPX-177839 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
[LysW]-L-2-aminoadipate 6-phosphate reductase Chain: A
Molecule details ›
Chain: A
Length: 345 amino acids
Theoretical weight: 38.28 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SH26 (Residues: 1-345; Coverage: 100%)
Gene names: TTHA1904, lysY
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P6222
Unit cell:
a: 144.957Å b: 144.957Å c: 85.128Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.185 0.207
Expression system: Escherichia coli