PDBe 5i94

X-ray diffraction
2.98Å resolution

Crystal structure of human glutaminase C in complex with the inhibitor UPGL-00019

Released:
Source organism: Homo sapiens

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 tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaminase kidney isoform, mitochondrial 65 kDa chain Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 539 amino acids
Theoretical weight: 59.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O94925 (Residues: 72-550; Coverage: 72%)
  • Best match: O94925-2 (Residues: 72-161)
Gene names: GLS, GLS1, KIAA0838
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P21
Unit cell:
a: 49.44Å b: 137.79Å c: 175.755Å
α: 90° β: 94.68° γ: 90°
R-values:
R R work R free
0.176 0.173 0.231
Expression system: Escherichia coli