PDBe 3czd

X-ray diffraction
2.4Å resolution

Crystal structure of human glutaminase in complex with L-glutamate

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaminase kidney isoform, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 315 amino acids
Theoretical weight: 34.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O94925 (Residues: 221-533; Coverage: 47%)
Gene names: GLS, GLS1, KIAA0838
Sequence domains: Glutaminase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: I4122
Unit cell:
a: 139.52Å b: 139.52Å c: 153.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.189 0.21
Expression system: Escherichia coli