PDBe 2dpl

X-ray diffraction
1.43Å resolution

Crystal Structure of the GMP synthase from Pyrococcus horikoshii OT3

Released:
Source organism: Pyrococcus horikoshii OT3
Entry authors: Asada Y, Kunishima N, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed:
(1a) L-glutamine + H(2)O = L-glutamate + NH(4)(+)
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GMP synthase [glutamine-hydrolyzing] subunit B Chains: A, B
Molecule details ›
Chains: A, B
Length: 308 amino acids
Theoretical weight: 34.61 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
  • Canonical: O59072 (Residues: 1-308; Coverage: 100%)
Gene names: PH1347, guaAB
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P212121
Unit cell:
a: 70.4Å b: 83.334Å c: 112.255Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.236 0.249
Expression system: Escherichia coli