› 1hnn

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF HUMAN PNMT COMPLEXED WITH SK&F 29661 AND ADOHCY(SAH)

Released:
DOI: 10.2210/pdb1hnn/pdb
PDB entry 1hnn coloured by chain, front view.
PDB entry 1hnn coloured by chain, side view.
PDB entry 1hnn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Getting the adrenaline going: crystal structure of the adrenaline-synthesizing enzyme PNMT.
Martin JL, Begun J, McLeish MJ, Caine JM, Grunewald GL
Structure 9 977-85 (2001)
PMID: 11591352

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145654 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylethanolamine N-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 282 amino acids
Theoretical weight: 30.89 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 SKF 2 x SKF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 94.35Å b: 94.35Å c: 187.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.23 0.273
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

13 mentions without citation

Many paths to methyltransfer: a chronicle of convergence.
Schubert et al. (2003)
12 more