› 3ih8

X-ray diffraction
2.3Å resolution

Crystal Structure Analysis of Mglu in its native form

Released:
DOI: 10.2210/pdb3ih8/pdb
PDB entry 3ih8 coloured by chain, front view.
PDB entry 3ih8 coloured by chain, side view.
PDB entry 3ih8 coloured by chain, top view.
Source organism: Micrococcus luteus
Primary publication:
Crystal structure of salt-tolerant glutaminase from Micrococcus luteus K-3 in the presence and absence of its product L-glutamate and its activator Tris.
Yoshimune K, Shirakihara Y, Wakayama M, Yumoto I
FEBS J 277 738-48 (2010)
PMID: 20050917

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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175753 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaminase Chains: A, B
Molecule details ›
Chains: A, B
Length: 456 amino acids
Theoretical weight: 48.3 KDa
Source organism: Micrococcus luteus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4U1A6 (Residues: 1-456; Coverage: 100%)
Gene name: glsA
Sequence domains: Glutaminase
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: C2
Unit cell:
a: 118.076Å b: 142.251Å c: 74.248Å
α: 90° β: 104.08° γ: 90°
R-values:
R R work R free
0.247 0.247 0.291
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Recent advances in microbial glutaminase production and applications-a concise review.
Amobonye et al. (2019)
1 more

1 mention without citation

The Glutaminase-Dependent System Confers Extreme Acid Resistance to New Species and Atypical Strains of Brucella.
Freddi et al. (2017)