› 1jqd

X-ray diffraction
2.28Å resolution

Crystal Structure Analysis of Human Histamine Methyltransferase (Thr105 Polymorphic Variant) Complexed with AdoHcy and Histamine

Released:
DOI: 10.2210/pdb1jqd/pdb
PDB entry 1jqd coloured by chain, front view.
PDB entry 1jqd coloured by chain, side view.
PDB entry 1jqd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Two polymorphic forms of human histamine methyltransferase: structural, thermal, and kinetic comparisons.
Horton JR, Sawada K, Nishibori M, Zhang X, Cheng X
Structure 9 837-49 (2001)
PMID: 11566133

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


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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P6
Unit cell:
a: 131.75Å b: 131.75Å c: 64.03Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.205 0.257
Expression system: Escherichia coli

Quick links

Citations

10 review citations

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

6 mentions without citation

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