PDBe 5jyo

X-ray diffraction
2.1Å resolution

Allosteric inhibition of Kidney Isoform of Glutaminase

Released:
Source organism: Homo sapiens
Primary publication:
Allosteric inhibition of KGA
Oncotarget (2016)

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

Assemblies composition:
monomeric (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaminase kidney isoform, mitochondrial 65 kDa chain Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 333 amino acids
Theoretical weight: 36.63 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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P1
Unit cell:
a: 126.404Å b: 126.629Å c: 126.269Å
α: 112.88° β: 102.81° γ: 112.74°
R-values:
R R work R free
0.19 0.19 0.213
Expression system: Escherichia coli