› 2aox

X-ray diffraction
3.12Å resolution

Histamine Methyltransferase (Primary Variant T105) Complexed with the Acetylcholinesterase Inhibitor and Altzheimer's Disease Drug Tacrine

Released:
DOI: 10.2210/pdb2aox/pdb
PDB entry 2aox coloured by chain, front view.
PDB entry 2aox coloured by chain, side view.
PDB entry 2aox coloured by chain, top view.
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 353 334-344 (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)
Assembly name:
PDBe Complex ID:
PDB-CPX-156132 (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: 33.33 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: 132.34Å b: 132.34Å c: 64.58Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.235 0.229 0.285
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Drug interactions.
Boobis et al. (2009)
3 more

1 mention without citation

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