X-ray diffraction
2.35Å resolution

Crystal structure of Methanoperedens nitroreducens elongation factor 2 bound to GMPPCP and magnesium

Primary publication:
Structural basis of elongation factor 2 switching
Curr Res Struct Biol 2 25-34 (2020)

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Elongation factor 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 732 amino acids
Theoretical weight: 80.84 KDa
Source organism: Candidatus Methanoperedens nitroreducens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: A0A062V290 (Residues: 1-729; Coverage: 100%)
Gene names: ANME2D_00299, fusA
Sequence domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 93.699Å b: 134.375Å c: 150.485Å
α: 90° β: 90° γ: 90°
R R work R free
0.171 0.168 0.224
Expression system: Escherichia coli BL21(DE3)