X-ray diffraction
1.5Å resolution

Crystal structure of Lys49 to Arg mutant of Diphthine synthase

Source organism: Pyrococcus horikoshii OT3
Entry authors: Mizutani H, Matsuura Y, Krishna Swamy BS, Simanshu DK, Murthy MRN, Kunishima N

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Diphthine synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 265 amino acids
Theoretical weight: 29.64 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
  • Canonical: O58456 (Residues: 1-265; Coverage: 100%)
Gene names: PH0725, dph5, dphB
Sequence domains: Tetrapyrrole (Corrin/Porphyrin) Methylases
Structure domains:

Ligands and Environments

Cofactor: Ligand SAH 1 x SAH
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P41212
Unit cell:
a: 104.501Å b: 104.501Å c: 137.523Å
α: 90° β: 90° γ: 90°
R R work R free
0.197 0.196 0.206
Expression system: Escherichia coli