› 5jyo

X-ray diffraction
2.1Å resolution

Allosteric inhibition of Kidney Isoform of Glutaminase

Released:
DOI: 10.2210/pdb5jyo/pdb
PDB entry 5jyo coloured by chain, front view.
PDB entry 5jyo coloured by chain, side view.
PDB entry 5jyo coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for exploring the allosteric inhibition of human kidney type glutaminase.
Ramachandran S, Pan CQ, Zimmermann SC, Duvall B, Tsukamoto T, Low BC, Sivaraman J
Oncotarget 7 57943-57954 (2016)
PMID: 27462863

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

Assemblies composition:
monomeric (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-131794 (preferred)
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:
Ligand 63J 4 x 63J
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

Quick links

Citations

7 review citations

Targeting cancer metabolism in the era of precision oncology.
Stine et al. (2022)
6 more

5 mentions without citation

A tale of two glutaminases: homologous enzymes with distinct roles in tumorigenesis.
Katt et al. (2017)
4 more