PDBe 2vdc

Electron Microscopy
9.5Å resolution

THE 9.5 A RESOLUTION STRUCTURE OF GLUTAMATE SYNTHASE FROM CRYO-ELECTRON MICROSCOPY AND ITS OLIGOMERIZATION BEHAVIOR IN SOLUTION: FUNCTIONAL IMPLICATIONS.

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero 12-mer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutamate synthase [NADPH] large chain Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 1472 amino acids
Theoretical weight: 161.62 KDa
Source organism: Azospirillum brasilense
Expression system: Escherichia coli
UniProt:
  • Canonical: Q05755 (Residues: 37-1508; Coverage: 97%)
Gene name: gltB
Sequence domains:
Glutamate synthase [NADPH] small chain Chains: G, H, I, J, K, L
Molecule details ›
Chains: G, H, I, J, K, L
Length: 456 amino acids
Theoretical weight: 49.37 KDa
Source organism: Azospirillum brasilense
Expression system: Escherichia coli
UniProt:
  • Canonical: Q05756 (Residues: 27-482; Coverage: 95%)
Gene name: gltD
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase

Ligands and Environments


Cofactor: Ligand FMN 6 x FMN

Cofactor: Ligand FAD 6 x FAD

No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 9.5Å
Relevant EMDB volumes: EMD-1440
Expression system: Escherichia coli