2eju

X-ray diffraction
1.95Å resolution

Complex structure of Trm1 from Pyrococcus horikoshii with S-adenosyl-L-Homocystein

Released:

Function and Biology Details

Reaction catalysed:
2 S-adenosyl-L-methionine + guanine(26) in tRNA = 2 S-adenosyl-L-homocysteine + N(2)-dimethylguanine(26) in tRNA
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA (guanine(26)-N(2))-dimethyltransferase Chain: A
Molecule details ›
Chain: A
Length: 378 amino acids
Theoretical weight: 43.01 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
  • Canonical: O59493 (Residues: 4-381; Coverage: 99%)
Gene names: PH1829, trm1
Sequence domains: N2,N2-dimethylguanosine tRNA methyltransferase
Structure domains:

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: C2221
Unit cell:
a: 74.781Å b: 109.655Å c: 96.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.246
Expression system: Escherichia coli