1v4a

X-ray diffraction
2Å resolution

Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase

Released:

Function and Biology Details

Reactions catalysed:
ATP + [glutamine synthetase]-L-tyrosine = diphosphate + [glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine
[Glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme Chain: A
Molecule details ›
Chain: A
Length: 440 amino acids
Theoretical weight: 51.04 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P30870 (Residues: 1-440; Coverage: 47%)
Gene names: JW3025, b3053, glnE
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3221
Unit cell:
a: 116.836Å b: 116.836Å c: 67.744Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.228 0.269
Expression system: Escherichia coli