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Atomistry » Chlorine » PDB 1jfv-1k73 » 1jqe » |
Chlorine in PDB 1jqe: Crystal Structure Analysis of Human Histamine Methyltransferase (ILE105 Polymorphic Variant) Complexed with Adohcy and Antimalarial Drug QuinacrineEnzymatic activity of Crystal Structure Analysis of Human Histamine Methyltransferase (ILE105 Polymorphic Variant) Complexed with Adohcy and Antimalarial Drug Quinacrine
All present enzymatic activity of Crystal Structure Analysis of Human Histamine Methyltransferase (ILE105 Polymorphic Variant) Complexed with Adohcy and Antimalarial Drug Quinacrine:
2.1.1.8; Protein crystallography data
The structure of Crystal Structure Analysis of Human Histamine Methyltransferase (ILE105 Polymorphic Variant) Complexed with Adohcy and Antimalarial Drug Quinacrine, PDB code: 1jqe
was solved by
J.R.Horton,
K.Sawada,
M.Nishibori,
X.Zhang,
X.Cheng,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure Analysis of Human Histamine Methyltransferase (ILE105 Polymorphic Variant) Complexed with Adohcy and Antimalarial Drug Quinacrine
(pdb code 1jqe). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure Analysis of Human Histamine Methyltransferase (ILE105 Polymorphic Variant) Complexed with Adohcy and Antimalarial Drug Quinacrine, PDB code: 1jqe: Chlorine binding site 1 out of 1 in 1jqeGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure Analysis of Human Histamine Methyltransferase (ILE105 Polymorphic Variant) Complexed with Adohcy and Antimalarial Drug Quinacrine
![]() Mono view ![]() Stereo pair view
Reference:
J.R.Horton,
K.Sawada,
M.Nishibori,
X.Zhang,
X.Cheng.
Two Polymorphic Forms of Human Histamine Methyltransferase: Structural, Thermal, and Kinetic Comparisons. Structure V. 9 837 2001.
Page generated: Thu Jul 10 17:35:49 2025
ISSN: ISSN 0969-2126 PubMed: 11566133 DOI: 10.1016/S0969-2126(01)00643-8 |
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