8imb

Electron Microscopy
2.9Å resolution

Filament interface structure of GAC with phosphate

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for activation and filamentation of glutaminase.
Cell Res 34 76-79 (2024)
PMID: 37833360
Related structures: EMD-35574

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)
PDBe Complex ID:
PDB-CPX-131797 (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: 476 amino acids
Theoretical weight: 53.08 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: O94925 (Residues: 123-550; Coverage: 64%)
Gene names: GLS, GLS1, KIAA0838
Sequence domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.9Å
Relevant EMDB volumes: EMD-35574
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'