› 1xcl

X-ray diffraction
2Å resolution

Guanidinoacetate methyltransferase containing S-adenosylhomocysteine and guanidine

Released:
DOI: 10.2210/pdb1xcl/pdb
PDB entry 1xcl coloured by chain, front view.
PDB entry 1xcl coloured by chain, side view.
PDB entry 1xcl coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Catalytic mechanism of guanidinoacetate methyltransferase: crystal structures of guanidinoacetate methyltransferase ternary complexes.
Komoto J, Yamada T, Takata Y, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F
Biochemistry 43 14385-94 (2004)
PMID: 15533043

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145503 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanidinoacetate N-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 235 amino acids
Theoretical weight: 26.27 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P10868 (Residues: 2-236; Coverage: 100%)
Gene name: Gamt
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P1
Unit cell:
a: 36.157Å b: 41.388Å c: 42.574Å
α: 104.24° β: 112.89° γ: 104.16°
R-values:
R R work R free
0.205 0.204 0.292
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Architectures, mechanisms and molecular evolution of natural product methyltransferases.
Liscombe et al. (2012)
2 more