5wj6

X-ray diffraction
2.44Å resolution

Crystal structure of glutaminase C in complex with inhibitor 2-phenyl-N-{5-[4-({5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl}amino)piperidin-1-yl]-1,3,4-thiadiazol-2-yl}acetamide (UPGL-00004)

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutaminase kidney isoform, mitochondrial 65 kDa chain Chains: A, C, D
Molecule details ›
Chains: A, 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: O94925-3 (Residues: 72-598)
Gene names: GLS, GLS1, KIAA0838
Sequence domains:
Glutaminase kidney isoform, mitochondrial 65 kDa chain Chain: B
Molecule details ›
Chain: B
Length: 539 amino acids
Theoretical weight: 59.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O94925 (Residues: 72-550; Coverage: 72%)
  • Best match: O94925-3 (Residues: 72-598)
Gene names: GLS, GLS1, KIAA0838
Sequence domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P212121
Unit cell:
a: 97.652Å b: 138.01Å c: 175.769Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.18 0.223
Expression system: Escherichia coli