› 1vhv

X-ray diffraction
1.75Å resolution

Function and Biology Details

Reaction catalysed: 
(1a) S-adenosyl-L-methionine + 2-((3S)-3-carboxy-3-aminopropyl)-L-histidine-[translation elongation factor 2] = S-adenosyl-L-homocysteine + 2-((3S)-3-carboxy-3-(methylamino)propyl)-L-histidine-[translation elongation factor 2]
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128175 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Diphthine synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 268 amino acids
Theoretical weight: 30.22 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli
UniProt:
  • Canonical: O29866 (Residues: 2-251; Coverage: 100%)
Gene names: AF_0381, dphB
Sequence domains: Tetrapyrrole (Corrin/Porphyrin) Methylases
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P21
Unit cell:
a: 50.892Å b: 56.416Å c: 101.144Å
α: 90° β: 100.78° γ: 90°
R-values:
R R work R free
0.211 0.211 0.254
Expression system: Escherichia coli

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Citations

23 review citations

Regulation of fatty acid metabolism in bacteria.
Fujita et al. (2007)
22 more