PDBe 4lni

X-ray diffraction
2.58Å resolution

B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of the transition state complex

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo 12-mer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine synthetase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 443 amino acids
Theoretical weight: 50.21 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P12425 (Residues: 2-444; Coverage: 100%)
Gene names: BSU17460, glnA
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P1
Unit cell:
a: 110.2Å b: 141.6Å c: 142.1Å
α: 60.29° β: 67.38° γ: 76.2°
R-values:
R R work R free
0.166 0.165 0.223
Expression system: Escherichia coli