› 8bsn

X-ray diffraction
2.49Å resolution

Function and Biology Details

Reaction catalysed: 
L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131797 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaminase kidney isoform, mitochondrial 65 kDa chain Chain: A
Molecule details ›
Chain: A
Length: 315 amino acids
Theoretical weight: 34.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O94925 (Residues: 221-533; Coverage: 47%)
Gene names: GLS, GLS1, KIAA0838
Sequence domains: Glutaminase

Ligands and Environments

2 bound ligands:
Ligand SO4 5 x SO4
Ligand R0C 1 x R0C
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: I4122
Unit cell:
a: 140.484Å b: 140.484Å c: 157.398Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.204 0.211
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Targeting Glutaminolysis: New Perspectives to Understand Cancer Development and Novel Strategies for Potential Target Therapies.
Wang et al. (2020)
1 more