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2ywb

X-ray diffraction
2.1Å resolution

Crystal structure of GMP synthetase from Thermus thermophilus

Released:
Model geometry
Fit model/data
Source organism: Thermus thermophilus HB8
Entry authors: Baba S, Kanagawa M, Yanai H, Ishii T, Kuramitsu S, Yokoyama S, Sampei G, Kawai G, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed:
XMP + L-glutamine + ATP + H2O = GMP + L-glutamate + AMP + diphosphate +2 H(+).
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
PDBe Complex ID:
PDB-CPX-177928 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GMP synthase [glutamine-hydrolyzing] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 503 amino acids
Theoretical weight: 55.89 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SI28 (Residues: 1-503; Coverage: 100%)
Gene names: TTHA1552, guaA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: C2
Unit cell:
a: 140.949Å b: 114.854Å c: 160.033Å
α: 90° β: 93.37° γ: 90°
R-values:
R R work R free
0.233 0.233 0.272
Expression system: Escherichia coli