3tqi

X-ray diffraction
2.84Å resolution

Structure of the GMP synthase (guaA) from Coxiella burnetii

Released:

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

Assemblies composition:
homo dimer (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GMP synthase [glutamine-hydrolyzing] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 527 amino acids
Theoretical weight: 59.03 KDa
Source organism: Coxiella burnetii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q83BZ6 (Residues: 1-524; Coverage: 100%)
Gene names: CBU_1341, guaA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 74.913Å b: 143.953Å c: 107.885Å
α: 90° β: 97.66° γ: 90°
R-values:
R R work R free
0.247 0.245 0.281
Expression system: Escherichia coli BL21(DE3)