› 1i7q

X-ray diffraction
1.95Å resolution

Function and Biology Details

Reaction catalysed: 
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133674 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Anthranilate synthase component 1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 519 amino acids
Theoretical weight: 57.66 KDa
Source organism: Serratia marcescens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00897 (Residues: 1-519; Coverage: 100%)
Gene name: trpE
Sequence domains:
Structure domains: Anthranilate synthase
Anthranilate synthase component 2 Chains: B, D
Molecule details ›
Chains: B, D
Length: 193 amino acids
Theoretical weight: 20.95 KDa
Source organism: Serratia marcescens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00900 (Residues: 1-193; Coverage: 100%)
Gene name: trpG
Sequence domains: Glutamine amidotransferase class-I
Structure domains: Rossmann fold

Ligands and Environments

4 bound ligands:
Ligand MG 2 x MG
Ligand BEZ 2 x BEZ
Ligand PYR 2 x PYR
Ligand GLU 2 x GLU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P21
Unit cell:
a: 87.316Å b: 68.984Å c: 116.363Å
α: 90° β: 108.52° γ: 90°
R-values:
R R work R free
0.181 0.181 0.246
Expression system: Escherichia coli

Quick links

Citations

8 review citations

A Three-Ring Circus: Metabolism of the Three Proteogenic Aromatic Amino Acids and Their Role in the Health of Plants and Animals.
Parthasarathy et al. (2018)
7 more

14 mentions without citation

Unraveling the Structure and Mechanism of the MST(ery) Enzymes.
Shelton et al. (2018)
13 more