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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:

Resolution Low / High (Å) 15.00 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.308, 73.830, 92.490, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 23.2

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 2zm1

Go back to Chlorine Binding Sites List in 2zm1
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

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Imidazo Pyrazin 1 Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl513

b:9.0
occ:1.00
 CL23 A:KSF513 0.0 9.0 1.0
C18 A:KSF513 1.8 3.2 1.0
C19 A:KSF513 2.8 4.8 1.0
C17 A:KSF513 2.8 3.9 1.0
N16 A:KSF513 3.1 2.9 1.0
C2 A:KSF513 3.4 2.0 1.0
CB A:ALA271 3.6 2.0 1.0
OG1 A:THR316 3.7 2.0 1.0
N A:LYS273 3.7 2.0 1.0
N3 A:KSF513 3.7 2.2 1.0
CB A:LYS273 3.8 2.0 1.0
O A:ALA271 3.9 2.4 1.0
O A:ILE314 4.0 2.0 1.0
CG2 A:THR316 4.0 2.0 1.0
C A:ALA271 4.0 2.0 1.0
C20 A:KSF513 4.1 4.1 1.0
C22 A:KSF513 4.1 3.4 1.0
O A:HOH679 4.1 8.0 1.0
C1 A:KSF513 4.2 2.0 1.0
C A:VAL272 4.3 2.0 1.0
CA A:LYS273 4.3 2.0 1.0
N A:VAL272 4.3 2.0 1.0
CG1 A:VAL259 4.4 3.3 1.0
CB A:THR316 4.4 2.0 1.0
CA A:ALA271 4.5 2.0 1.0
CA A:VAL272 4.6 2.0 1.0
N A:THR316 4.6 2.0 1.0
C21 A:KSF513 4.6 2.1 1.0
C4 A:KSF513 4.6 2.0 1.0
C9 A:KSF513 4.9 2.0 1.0
C A:ILE314 4.9 2.0 1.0

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.
ISSN: ISSN 0968-0896
PubMed: 18977146
DOI: 10.1016/J.BMC.2008.10.041
Page generated: Sat Jul 20 15:34:33 2024

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