› 2aow

X-ray diffraction
2.97Å resolution

Histamine Methyltransferase (Natural Variant I105) Complexed with the Acetylcholinesterase Inhibitor and Altzheimer's Disease Drug Tacrine

Released:
DOI: 10.2210/pdb2aow/pdb
PDB 2aow coloured by chain and viewed from the front.
PDB 2aow coloured by chain and viewed from the side.
PDB 2aow coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Structural basis for inhibition of histamine N-methyltransferase by diverse drugs.
Horton JR, Sawada K, Nishibori M, Cheng X
J. Mol. Biol. 353 334-44 (2005)
PMID: 16168438

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + histamine = S-adenosyl-L-homocysteine + N(tau)-methylhistamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histamine N-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 292 amino acids
Theoretical weight: 33.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P50135 (Residues: 1-292; Coverage: 100%)
Gene name: HNMT
Sequence domains: Methyltransferase domain
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments

1 bound ligand:
Ligand THA 2 x THA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P6
Unit cell:
a: 132.96Å b: 132.96Å c: 65.21Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.224 0.219 0.269
Expression system: Escherichia coli

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Citations

4 review citations

Inhibition of Astrocytic Histamine N-Methyltransferase as a Possible Target for the Treatment of Alzheimer's Disease.
Flores-Clemente et al. (2021)
3 more

1 mention without citation

Structural basis for inhibition of histamine N-methyltransferase by diverse drugs.
Horton et al. (2005)