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Chlorine in PDB 2ito: Crystal Structure of Egfr Kinase Domain G719S Mutation in Complex with Iressa

Enzymatic activity of Crystal Structure of Egfr Kinase Domain G719S Mutation in Complex with Iressa

All present enzymatic activity of Crystal Structure of Egfr Kinase Domain G719S Mutation in Complex with Iressa:
2.7.10.1;

Protein crystallography data

The structure of Crystal Structure of Egfr Kinase Domain G719S Mutation in Complex with Iressa, PDB code: 2ito was solved by C.-H.Yun, T.J.Boggon, Y.Li, S.Woo, H.Greulich, M.Meyerson, M.J.Eck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.51 / 3.25
Space group I 2 3
Cell size a, b, c (Å), α, β, γ (°) 142.929, 142.929, 142.929, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 26.6

Other elements in 2ito:

The structure of Crystal Structure of Egfr Kinase Domain G719S Mutation in Complex with Iressa also contains other interesting chemical elements:

Fluorine (F) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Egfr Kinase Domain G719S Mutation in Complex with Iressa (pdb code 2ito). 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 Egfr Kinase Domain G719S Mutation in Complex with Iressa, PDB code: 2ito:

Chlorine binding site 1 out of 1 in 2ito

Go back to Chlorine Binding Sites List in 2ito
Chlorine binding site 1 out of 1 in the Crystal Structure of Egfr Kinase Domain G719S Mutation in Complex with Iressa


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 Egfr Kinase Domain G719S Mutation in Complex with Iressa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2020

b:89.8
occ:1.00
 CL A:IRE2020 0.0 89.8 1.0
CAX A:IRE2020 1.7 89.0 1.0
CAG A:IRE2020 2.7 89.2 1.0
CAW A:IRE2020 2.7 89.1 1.0
FAB A:IRE2020 2.9 88.8 1.0
O A:LEU788 3.3 69.3 1.0
CG2 A:THR790 3.3 63.1 1.0
N A:LYS745 3.5 85.4 1.0
CB A:LYS745 3.5 88.3 1.0
CB A:LEU788 3.7 73.1 1.0
C A:LEU788 3.9 70.6 1.0
CB A:THR790 4.0 63.9 1.0
CAY A:IRE2020 4.0 89.1 1.0
N A:THR790 4.0 64.8 1.0
CAD A:IRE2020 4.0 89.5 1.0
CA A:LYS745 4.1 89.0 1.0
O A:ALA743 4.2 73.8 1.0
C A:ILE744 4.4 81.8 1.0
CD2 A:LEU788 4.4 73.8 1.0
CA A:LEU788 4.4 73.0 1.0
CAE A:IRE2020 4.5 89.2 1.0
CA A:ILE744 4.5 79.4 1.0
N A:ILE789 4.5 68.6 1.0
C A:ALA743 4.6 74.2 1.0
CG A:LEU788 4.6 73.0 1.0
CA A:THR790 4.6 63.9 1.0
C A:ILE789 4.7 65.7 1.0
N A:ILE744 4.7 76.5 1.0
CA A:ILE789 4.7 66.9 1.0
CG A:LYS745 4.8 86.2 1.0
CE A:LYS745 4.9 81.4 1.0
N1 A:IRE2020 5.0 89.4 1.0

Reference:

C.-H.Yun, T.J.Boggon, Y.Li, S.Woo, H.Greulich, M.Meyerson, M.J.Eck. Structures of Lung Cancer-Derived Egfr Mutants and Inhibitor Complexes: Mechanism of Activation and Insights Into Differential Inhibitor Sensitivity Cancer Cell V. 11 217 2007.
ISSN: ISSN 1535-6108
PubMed: 17349580
DOI: 10.1016/J.CCR.2006.12.017
Page generated: Sat Dec 12 09:09:12 2020

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