PDBe 4bqm

X-ray diffraction
2.18Å resolution

Crystal structure of human liver-type glutaminase, catalytic domain

Released:
Source organism: Homo sapiens
Entry authors: Ferreira IM, Vollmar M, Krojer T, Strain-Damerell C, Froese S, Coutandin D, Williams E, Burgess-Brown N, von Delft F, Arrowsmith CH, Bountra C, Edwards A, Dias SMG, Ambrosio ALB, Yue WW

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 liver isoform, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 349 amino acids
Theoretical weight: 38.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UI32 (Residues: 154-479; Coverage: 54%)
Gene names: GA, GLS2
Sequence domains: Glutaminase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: R32
Unit cell:
a: 203.613Å b: 203.613Å c: 98.965Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.177 0.203
Expression system: Escherichia coli BL21(DE3)