1JQD

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

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.28 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.205 
  • R-Value Observed: 0.211 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history. 


Literature

Two polymorphic forms of human histamine methyltransferase: structural, thermal, and kinetic comparisons.

Horton, J.R., Sawada, K., Nishibori, M., Zhang, X., Cheng, X.

(2001) Structure 9: 837-849

  • DOI: https://doi.org/10.1016/s0969-2126(01)00643-8
  • Primary Citation of Related Structures:  
    1JQD, 1JQE

  • 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.

    • Organizational Affiliation: 

    Department of Biochemistry, Emory University School of Medicine, 1510 Clifton Road, Atlanta, GA 30322, USA.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Histamine N-Methyltransferase
A, B
292Homo sapiensMutation(s): 0 
Gene Names: HNMT
EC: 2.1.1.8
UniProt & NIH Common Fund Data Resources
Find proteins for P50135 (Homo sapiens)
Explore P50135 
Go to UniProtKB:  P50135
PHAROS:  P50135
GTEx:  ENSG00000150540 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP50135
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
SAH BindingDB:  1JQD Ki: min: 1.05e+4, max: 1.81e+4 (nM) from 2 assay(s)
Binding MOAD:  1JQD Ki: 6900 (nM) from 1 assay(s)
PDBBind:  1JQD Ki: 6900 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.28 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.205 
  • R-Value Observed: 0.211 
  • Space Group: P 6
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 131.75α = 90
b = 131.75β = 90
c = 64.03γ = 120
Software Package:
Software NamePurpose
CNSrefinement
MAR345data collection
SCALEPACKdata scaling
CNSphasing

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-08-06
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-04
    Changes: Refinement description
  • Version 1.4: 2024-02-07
    Changes: Data collection, Database references, Derived calculations
  • Version 1.5: 2024-04-03
    Changes: Refinement description