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Atomistry » Chlorine » PDB 2zhp-3a34 » 2zm1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 2zhp-3a34 » 2zm1 » |
Chlorine in PDB 2zm1: Crystal Structure of Imidazo Pyrazin 1 Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394)Enzymatic activity of Crystal Structure of Imidazo Pyrazin 1 Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394)
All present enzymatic activity of Crystal Structure of Imidazo Pyrazin 1 Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394):
2.7.10.2; Protein crystallography data
The structure of Crystal Structure of Imidazo Pyrazin 1 Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394), PDB code: 2zm1
was solved by
E.Tsuji,
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 of Imidazo Pyrazin 1 Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394)
(pdb code 2zm1). 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 of Imidazo Pyrazin 1 Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394), PDB code: 2zm1: Chlorine binding site 1 out of 1 in 2zm1Go back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of Imidazo Pyrazin 1 Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394)
![]() Mono view ![]() Stereo pair view
Reference:
T.Ozawa,
E.Tsuji,
M.Ozawa,
C.Handa,
H.Mukaiyama,
T.Nishimura,
S.Kobayashi,
K.Okazaki.
The Importance of Ch/Pi Hydrogen Bonds in Rational Drug Design: An Ab Initio Fragment Molecular Orbital Study to Leukocyte-Specific Protein Tyrosine (Lck) Kinase Bioorg.Med.Chem. V. 16 10311 2008.
Page generated: Fri Jul 11 02:55:16 2025
ISSN: ISSN 0968-0896 PubMed: 18977146 DOI: 10.1016/J.BMC.2008.10.041 |
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