› 5do0

X-ray diffraction
2.6Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-517530 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
protein lysine methyltransferase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 554 amino acids
Theoretical weight: 63.48 KDa
Source organism: Rickettsia prowazekii str. Madrid E
Expression system: Escherichia coli
UniProt:
  • Canonical: O05979 (Residues: 1-553; Coverage: 100%)
Gene name: RP789
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 98.498Å b: 62.466Å c: 107.853Å
α: 90° β: 100.78° γ: 90°
R-values:
R R work R free
0.215 0.214 0.243
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The enigmatic biology of rickettsiae: recent advances, open questions and outlook.
McGinn et al. (2021)
2 more

1 mention without citation

Structural Insights into Substrate Recognition and Catalysis in Outer Membrane Protein B (OmpB) by Protein-lysine Methyltransferases from Rickettsia.
Abeykoon et al. (2016)