3lzd

X-ray diffraction
2.1Å resolution

Crystal structure of Dph2 from Pyrococcus horikoshii with 4Fe-4S cluster

Released:

Function and Biology Details

Reaction catalysed:
L-histidine-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-((3S)-3-amino-3-carboxypropyl)-L-histidine-[translation elongation factor 2] + S-methyl-5'-thioadenosine
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-(3-amino-3-carboxypropyl)histidine synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 378 amino acids
Theoretical weight: 42.54 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
  • Canonical: O58832 (Residues: 1-342; Coverage: 100%)
Gene names: PH1105, dph2
Sequence domains: Putative diphthamide synthesis protein
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 55.695Å b: 80.525Å c: 162.142Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.252
Expression system: Escherichia coli