X-ray diffraction
2.2Å resolution

Crystal structure of GMP synthetase from Thermus thermophilus in complex with XMP

Source organism: Thermus thermophilus HB8
Entry authors: Baba S, Kanagawa M, Kuramitsu S, Yokoyama S, Sampei G, Kawai G, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

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

Assemblies composition:
homo dimer (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
GMP synthase [glutamine-hydrolyzing] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 503 amino acids
Theoretical weight: 56.13 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
  • Canonical: Q5SI28 (Residues: 1-503; Coverage: 100%)
Gene names: TTHA1552, guaA
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: C2
Unit cell:
a: 142.58Å b: 115.213Å c: 159.348Å
α: 90° β: 93.21° γ: 90°
R R work R free
0.236 0.236 0.278
Expression system: Escherichia coli