› 3gdh

X-ray diffraction
2Å resolution

Methyltransferase domain of human Trimethylguanosine Synthase 1 (TGS1) bound to m7GTP and adenosyl-homocysteine (active form)

Released:
DOI: 10.2210/pdb3gdh/pdb
PDB entry 3gdh coloured by chain, front view.
PDB entry 3gdh coloured by chain, side view.
PDB entry 3gdh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for m7G-cap hypermethylation of small nuclear, small nucleolar and telomerase RNA by the dimethyltransferase TGS1.
Monecke T, Dickmanns A, Ficner R
Nucleic Acids Res 37 3865-77 (2009)
PMID: 19386620

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188737 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trimethylguanosine synthase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 241 amino acids
Theoretical weight: 26.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96RS0 (Residues: 618-853; Coverage: 28%)
Gene names: HCA137, NCOA6IP, PIMT, TGS1
Sequence domains: RNA cap guanine-N2 methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments

4 bound ligands:
Ligand MGP 3 x MGP
Ligand SAH 3 x SAH
Ligand PGR 4 x PGR
Ligand PGO 1 x PGO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: R3
Unit cell:
a: 156.248Å b: 156.248Å c: 100.309Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.18 0.213
Expression system: Escherichia coli

Quick links

Citations

10 review citations

PPARalpha: energy combustion, hypolipidemia, inflammation and cancer.
Pyper et al. (2010)
9 more

9 mentions without citation

RNA methyltransferases involved in 5' cap biosynthesis.
Byszewska et al. (2014)
8 more