3g5t

X-ray diffraction
1.12Å resolution

Crystal structure of trans-aconitate 3-methyltransferase from yeast

Released:
Source organism: Saccharomyces cerevisiae
Entry authors: Burgie ES, Bingman CA, Wesenberg GE, Phillips Jr GN, Center for Eukaryotic Structural Genomics (CESG)

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + trans-aconitate = S-adenosyl-L-homocysteine + (E)-2-(methoxycarbonylmethyl)butenedioate
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-152417 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trans-aconitate 3-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 299 amino acids
Theoretical weight: 35.05 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P32643 (Residues: 2-299; Coverage: 100%)
Gene names: SYGP-ORF63, TAM1, TMT1, YER175C
Sequence domains: Methyltransferase domain
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P212121
Unit cell:
a: 36.834Å b: 91.891Å c: 104.269Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.121 0.12 0.137
Expression system: Escherichia coli