6ujg

X-ray diffraction
3Å resolution

Crystal structure of human GAC in complex with inhibitor UPGL00012

Released:
Source organism: Homo sapiens
Entry authors: Huang Q, Cerione RA

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

Assembly composition:
homo tetramer (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: 527 amino acids
Theoretical weight: 58.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
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: P21
Unit cell:
a: 98.828Å b: 138.84Å c: 177.207Å
α: 90° β: 90.034° γ: 90°
R-values:
R R work R free
0.234 0.233 0.306
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'