› 8ooo

X-ray diffraction
2.15Å resolution

Glutamine synthetase from Methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and MgATP at 2.15 A resolution

Released:
DOI: 10.2210/pdb8ooo/pdb
PDB entry 8ooo coloured by chain, front view.
PDB entry 8ooo coloured by chain, side view.
PDB entry 8ooo coloured by chain, top view.
Source organism: Methanothermococcus thermolithotrophicus DSM 2095
Primary publication:
Differences in regulation mechanisms of glutamine synthetases from methanogenic archaea unveiled by structural investigations.
Müller MC, Lemaire ON, Kurth JM, Welte CU, Wagner T
OpenAccess logo Commun Biol 7 111 (2024)
PMID: 38243071

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-239146 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine synthetase from Methanothermococcus thermolithotrophicus 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: 448 amino acids
Theoretical weight: 50.3 KDa
Source organism: Methanothermococcus thermolithotrophicus DSM 2095

Ligands and Environments

8 bound ligands:
Ligand EDO 26 x EDO
Ligand PEG 10 x PEG
Ligand GOL 1 x GOL
Ligand ATP 12 x ATP
Ligand AKG 12 x AKG
Ligand MOE 2 x MOE
Ligand MG 3 x MG
Ligand PG4 2 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P1
Unit cell:
a: 112.337Å b: 131.773Å c: 131.507Å
α: 60.04° β: 87.72° γ: 67.34°
R-values:
R R work R free
0.183 0.182 0.214

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