6emv

X-ray diffraction
2.9Å resolution

Crystal Structure of dual specific Trm10 construct from Thermococcus kodakaraensis.

Released:

Function and Biology Details

Reactions catalysed:
S-adenosyl-L-methionine + adenine(9) in tRNA = S-adenosyl-L-homocysteine + N(1)-methyladenine(9) in tRNA
S-adenosyl-L-methionine + guanine(9) in tRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine(9) in tRNA
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA (guanine(9)-/adenine(9)-N1)-methyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 197 amino acids
Theoretical weight: 22.42 KDa
Source organism: Thermococcus kodakarensis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5JD38 (Residues: 97-272; Coverage: 48%)
Gene name: TK0422

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: P61
Unit cell:
a: 71.082Å b: 71.082Å c: 192.233Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.194 0.25
Expression system: Escherichia coli BL21(DE3)