2d7j

X-ray diffraction
1.89Å resolution

Crystal Structure Analysis of Glutamine Amidotransferase from Pyrococcus horikoshii OT3

Released:
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Crystal structure of glutamine amidotransferase from Pyrococcus horikoshii OT3
Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci. 81 459-462 (2005)

Function and Biology Details

Reaction catalysed:
(1a) L-glutamine + H(2)O = L-glutamate + NH(4)(+)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-129802 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GMP synthase [glutamine-hydrolyzing] subunit A Chain: A
Molecule details ›
Chain: A
Length: 209 amino acids
Theoretical weight: 23.72 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
  • Canonical: O59071 (Residues: 1-189; Coverage: 100%)
Gene names: PH1346, guaAA
Sequence domains: Glutamine amidotransferase class-I
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P3221
Unit cell:
a: 64.941Å b: 64.941Å c: 116.408Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.184 0.213
Expression system: Escherichia coli