X-ray diffraction
2.35Å resolution

Crystal structure of a GMP synthase (glutamine-hydrolyzing) from Neisseria gonorrhoeae

Source organism: Neisseria gonorrhoeae
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
GMP synthase [glutamine-hydrolyzing] Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 529 amino acids
Theoretical weight: 58.76 KDa
Source organism: Neisseria gonorrhoeae
Expression system: Escherichia coli
  • Canonical: B4RJH7 (Residues: 1-521; Coverage: 100%)
Gene names: NGK_2643, guaA
Sequence domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P1
Unit cell:
a: 108.39Å b: 109.35Å c: 109.91Å
α: 115.33° β: 100° γ: 108.06°
R R work R free
0.188 0.186 0.223
Expression system: Escherichia coli