› 4o7d

X-ray diffraction
2.3Å resolution

Crystal structure of human glutaminase in complex DON

Released:
DOI: 10.2210/pdb4o7d/pdb
PDB entry 4o7d coloured by chain, front view.
PDB entry 4o7d coloured by chain, side view.
PDB entry 4o7d coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the active site inhibition mechanism of human kidney-type glutaminase (KGA).
Thangavelu K, Chong QY, Low BC, Sivaraman J
Sci Rep 4 3827 (2014)
PMID: 24451979

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: 313 amino acids
Theoretical weight: 34.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O94925 (Residues: 221-531; Coverage: 47%)
Gene names: GLS, GLS1, KIAA0838
Sequence domains: Glutaminase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand ONL 1 x ONL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: I4122
Unit cell:
a: 139.278Å b: 139.278Å c: 155.502Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.193 0.211
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Targeting Glutamine Induces Apoptosis: A Cancer Therapy Approach.
Chen et al. (2015)
13 more

7 mentions without citation

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