1JQD

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

Summary for 1JQD

Entry DOI	10.2210/pdb1jqd/pdb
Related	1JQE
Descriptor	Histamine N-Methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, HISTAMINE, ... (4 entities in total)
Functional Keywords	classic methyltransferase fold, protein-substrate-cofactor complex, transferase
Biological source	Homo sapiens (human)
Cellular location	Cytoplasm : P50135
Total number of polymer chains	2
Total formula weight	67657.15
Authors	Horton, J.R.,Sawada, K.,Nishibori, M.,Zhang, X.,Cheng, X. (deposition date: 2001-08-06, release date: 2002-08-06, Last modification date: 2024-04-03)
Primary citation	Horton, J.R.,Sawada, K.,Nishibori, M.,Zhang, X.,Cheng, X. Two polymorphic forms of human histamine methyltransferase: structural, thermal, and kinetic comparisons. Structure, 9:837-849, 2001 Cited by PubMed Abstract: Histamine plays important biological roles in cell-to-cell communication; it is a mediator in allergic responses, a regulator of gastric acid secretion, a messenger in bronchial asthma, and a neurotransmitter in the central nervous system. Histamine acts by binding to histamine receptors, and its local action is terminated primarily by methylation. Human histamine N-methyltransferase (HNMT) has a common polymorphism at residue 105 that correlates with the high- (Thr) and low- (Ile) activity phenotypes. PubMed: 11566133 DOI: 10.1016/S0969-2126(01)00643-8 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.28 Å)

Structure validation