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X-ray diffraction
2.4Å resolution

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + phenylethanolamine = S-adenosyl-L-homocysteine + N-methylphenylethanolamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145655 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylethanolamine N-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 289 amino acids
Theoretical weight: 31.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11086 (Residues: 1-282; Coverage: 100%)
Gene names: PENT, PNMT
Sequence domains: NNMT/PNMT/TEMT family
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 2 x SAH
1 bound ligand:
Ligand ES2 2 x ES2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P43212
Unit cell:
a: 93.908Å b: 93.908Å c: 188.615Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.206 0.271
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Applications of isothermal titration calorimetry in pure and applied research--survey of the literature from 2010.
Ghai et al. (2012)
4 more

2 mentions without citation

Fragment-based screening by protein crystallography: successes and pitfalls.
Chilingaryan et al. (2012)
1 more