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X-ray diffraction
2.8Å resolution

The Crystal Structure of Glutamine Amidotransferase from Thermotoga maritima

Released:

Function and Biology Details

Reactions catalysed:
L-glutamine + H(2)O = L-glutamate + NH(3)
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-194696 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Imidazole glycerol phosphate synthase subunit HisH Chains: A, B
Molecule details ›
Chains: A, B
Length: 205 amino acids
Theoretical weight: 23.47 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9X0C8 (Residues: 1-201; Coverage: 100%)
Gene names: TM_1038, hisH
Sequence domains:
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3221
Unit cell:
a: 82.045Å b: 82.045Å c: 176.352Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.229 0.229 0.274
Expression system: Escherichia coli BL21(DE3)