› 1khh

X-ray diffraction
2.5Å resolution

Crystal Structure of Guanidinoacetate Methyltransferase from Rat Liver: A Template Structure of Protein Arginine Methyltransferase

Released:
DOI: 10.2210/pdb1khh/pdb
PDB entry 1khh coloured by chain, front view.
PDB entry 1khh coloured by chain, side view.
PDB entry 1khh coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of guanidinoacetate methyltransferase from rat liver: a model structure of protein arginine methyltransferase.
Komoto J, Huang Y, Takata Y, Yamada T, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F
J Mol Biol 320 223-35 (2002)
PMID: 12079381

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145504 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanidinoacetate N-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 198 amino acids
Theoretical weight: 22.56 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P10868 (Residues: 39-236; Coverage: 84%)
Gene name: Gamt
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 2 x SAH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43
Unit cell:
a: 54.25Å b: 54.25Å c: 156.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.214 0.284
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential.
Krause et al. (2007)
3 more

2 mentions without citation

Many paths to methyltransfer: a chronicle of convergence.
Schubert et al. (2003)
1 more