2ejt

X-ray diffraction
2.2Å resolution

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

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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-129868 (preferred)
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 SAM 1 x SAM
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: 74.755Å b: 109.414Å c: 96.671Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.236
Expression system: Escherichia coli