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Chlorine in PDB 4i23: Crystal Structure of the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked)

Enzymatic activity of Crystal Structure of the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked)

All present enzymatic activity of Crystal Structure of the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked):
2.7.10.1;

Protein crystallography data

The structure of Crystal Structure of the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked), PDB code: 4i23 was solved by K.S.Gajiwala, J.Feng, R.Ferre, K.Ryan, O.Brodsky, A.Stewart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.92 / 2.80
Space group I 2 3
Cell size a, b, c (Å), α, β, γ (°) 146.342, 146.342, 146.342, 90.00, 90.00, 90.00
R / Rfree (%) 47.6 / 29.8

Other elements in 4i23:

The structure of Crystal Structure of the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked) also contains other interesting chemical elements:

Fluorine (F) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked) (pdb code 4i23). 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 the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked), PDB code: 4i23:

Chlorine binding site 1 out of 1 in 4i23

Go back to Chlorine Binding Sites List in 4i23
Chlorine binding site 1 out of 1 in the Crystal Structure of the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked)


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 the Wild-Type Egfr Kinase Domain in Complex with Dacomitinib (Soaked) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl9001

b:89.3
occ:1.00
CL A:1C99001 0.0 89.3 1.0
C17 A:1C99001 1.7 88.9 1.0
C16 A:1C99001 2.7 88.1 1.0
C18 A:1C99001 2.8 88.5 1.0
F21 A:1C99001 3.0 88.9 1.0
OG1 A:THR790 3.1 56.6 1.0
CG2 A:THR790 3.5 52.7 1.0
O A:LEU788 3.5 52.9 1.0
O A:ALA743 3.6 57.4 1.0
CB A:LYS745 3.7 67.7 1.0
N A:THR790 3.8 51.0 1.0
C A:LEU788 3.8 54.7 1.0
CB A:LEU788 3.8 56.9 1.0
CB A:THR790 3.8 52.0 1.0
N A:LYS745 3.9 65.9 1.0
C15 A:1C99001 4.1 87.4 1.0
C19 A:1C99001 4.1 87.6 1.0
N A:ILE789 4.2 52.9 1.0
C A:ILE789 4.2 51.6 1.0
C A:ALA743 4.2 55.8 1.0
CA A:ILE789 4.3 51.9 1.0
CA A:THR790 4.4 51.4 1.0
CA A:LEU788 4.4 56.6 1.0
CA A:LYS745 4.4 71.0 1.0
C A:ILE744 4.6 61.6 1.0
C20 A:1C99001 4.6 87.8 1.0
CA A:ILE744 4.7 58.9 1.0
CB A:ALA743 4.7 51.6 1.0
N A:ILE744 4.7 58.2 1.0
CD A:LYS745 4.9 66.5 1.0
CG A:LYS745 4.9 66.8 1.0
O A:ILE789 5.0 51.2 1.0

Reference:

K.S.Gajiwala, J.Feng, R.Ferre, K.Ryan, O.Brodsky, S.Weinrich, J.C.Kath, A.Stewart. Insights Into the Aberrant Activity of Mutant Egfr Kinase Domain and Drug Recognition. Structure V. 21 209 2013.
ISSN: ISSN 0969-2126
PubMed: 23273428
DOI: 10.1016/J.STR.2012.11.014
Page generated: Sun Jul 21 16:20:55 2024

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