1jqe

X-ray diffraction
1.91Å resolution

Crystal Structure Analysis of Human Histamine Methyltransferase (Ile105 Polymorphic Variant) Complexed with AdoHcy and Antimalarial Drug Quinacrine

Released:

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + histamine = S-adenosyl-L-homocysteine + N(tau)-methylhistamine
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 33.35 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


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

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P6
Unit cell:
a: 130.34Å b: 130.34Å c: 63.01Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.195 0.235
Expression system: Escherichia coli