3pfh

X-ray diffraction
1.79Å resolution

X-Ray crystal structure the N,N-dimethyltransferase TylM1 from Streptomyces fradiae in complex with SAH and dTDP-Quip3N

Released:

Function and Biology Details

Reaction catalysed:
2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose = 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-161176 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase Chains: A, D
Molecule details ›
Chains: A, D
Length: 263 amino acids
Theoretical weight: 28.54 KDa
Source organism: Streptomyces fradiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P95748 (Residues: 1-255; Coverage: 100%)
Gene names: tylM1, tylMI
Sequence domains: Methyltransferase domain
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 86.624Å b: 41.123Å c: 87.293Å
α: 90° β: 117.93° γ: 90°
R-values:
R R work R free
0.212 0.209 0.266
Expression system: Escherichia coli BL21