› 5i94

X-ray diffraction
2.98Å resolution

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

Released:
DOI: 10.2210/pdb5i94/pdb
PDB entry 5i94 coloured by chain, front view.
PDB entry 5i94 coloured by chain, side view.
PDB entry 5i94 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Design and evaluation of novel glutaminase inhibitors.
McDermott LA, Iyer P, Vernetti L, Rimer S, Sun J, Boby M, Yang T, Fioravanti M, O'Neill J, Wang L, Drakes D, Katt W, Huang Q, Cerione R
Bioorg Med Chem 24 1819-39 (2016)
PMID: 26988803

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-522853 (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: O94925-3 (Residues: 72-598)
Gene names: GLS, GLS1, KIAA0838
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 69V 2 x 69V
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

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Citations

6 review citations

Endothelial Cell Metabolism.
Eelen et al. (2018)
5 more

3 mentions without citation

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