› 2p35

X-ray diffraction
1.95Å resolution

Crystal structure of trans-aconitate methyltransferase from Agrobacterium tumefaciens

Released:
DOI: 10.2210/pdb2p35/pdb
PDB 2p35 coloured by chain and viewed from the front.
PDB 2p35 coloured by chain and viewed from the side.
PDB 2p35 coloured by chain and viewed from the top.
Source organism: Agrobacterium fabrum str. C58
Entry authors: Chang C, Xu X, Zheng H, Savchenko A, Edwards AM, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + trans-aconitate = S-adenosyl-L-homocysteine + (E)-3-(methoxycarbonyl)pent-2-enedioate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trans-aconitate 2-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 259 amino acids
Theoretical weight: 29.12 KDa
Source organism: Agrobacterium fabrum str. C58
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8UH15 (Residues: 1-256; Coverage: 100%)
Gene names: AGR_C_1589, Atu0870, tam
Sequence domains: Methyltransferase domain
Structure domains:

Ligands and Environments


Cofactor: Ligand SAH 2 x SAH
No bound ligands
1 modified residue:
Ligand MSE 14 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P65
Unit cell:
a: 103.097Å b: 103.097Å c: 107.457Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.186 0.214
Expression system: Escherichia coli

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