› 1u60

X-ray diffraction
1.61Å resolution

Function and Biology Details

Reaction catalysed: 
L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-160168 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaminase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 310 amino acids
Theoretical weight: 32.93 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P77454 (Residues: 1-310; Coverage: 100%)
Gene names: JW0474, b0485, glsA1, ybaS
Sequence domains: Glutaminase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
Ligand EDO 12 x EDO
Ligand FMT 9 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 50.509Å b: 155.891Å c: 164.171Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.143 0.178
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Control of immune response by amino acid metabolism.
Grohmann et al. (2010)
6 more

5 mentions without citation

Functional and structural characterization of four glutaminases from Escherichia coli and Bacillus subtilis.
Brown et al. (2008)
4 more