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Chlorine in PDB 3poz: Egfr Kinase Domain Complexed with Tak-285

Enzymatic activity of Egfr Kinase Domain Complexed with Tak-285

All present enzymatic activity of Egfr Kinase Domain Complexed with Tak-285:
2.7.10.1;

Protein crystallography data

The structure of Egfr Kinase Domain Complexed with Tak-285, PDB code: 3poz was solved by K.Aertgeerts, R.Skene, S.Sogabe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.806, 68.881, 104.558, 90.00, 90.00, 90.00
R / Rfree (%) 21.9 / 24.3

Other elements in 3poz:

The structure of Egfr Kinase Domain Complexed with Tak-285 also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Egfr Kinase Domain Complexed with Tak-285 (pdb code 3poz). 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 Egfr Kinase Domain Complexed with Tak-285, PDB code: 3poz:

Chlorine binding site 1 out of 1 in 3poz

Go back to Chlorine Binding Sites List in 3poz
Chlorine binding site 1 out of 1 in the Egfr Kinase Domain Complexed with Tak-285


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Egfr Kinase Domain Complexed with Tak-285 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1023

b:23.9
occ:1.00
CL A:03P1023 0.0 23.9 1.0
C12 A:03P1023 1.8 20.4 1.0
C11 A:03P1023 2.7 19.0 1.0
C13 A:03P1023 2.7 24.1 1.0
O1 A:03P1023 3.0 22.9 1.0
O A:LEU788 3.2 27.0 1.0
CG2 A:THR790 3.5 22.1 1.0
CB A:LYS745 3.5 30.5 1.0
N A:LYS745 3.6 27.4 1.0
C A:LEU788 3.8 26.9 1.0
CB A:LEU788 3.9 29.0 1.0
O A:ALA743 3.9 24.5 1.0
C16 A:03P1023 4.0 22.1 1.0
C10 A:03P1023 4.0 22.7 1.0
C14 A:03P1023 4.0 21.4 1.0
CB A:THR790 4.1 26.1 1.0
C21 A:03P1023 4.2 22.7 1.0
CA A:LYS745 4.2 30.1 1.0
C A:ALA743 4.4 25.1 1.0
N A:THR790 4.4 23.3 1.0
N A:ILE789 4.4 26.4 1.0
C A:ILE744 4.4 28.9 1.0
CA A:LEU788 4.5 29.1 1.0
C15 A:03P1023 4.5 22.8 1.0
CA A:ILE744 4.6 26.3 1.0
C A:ILE789 4.6 22.7 1.0
CA A:ILE789 4.6 24.8 1.0
N A:ILE744 4.7 23.7 1.0
CG A:LYS745 4.8 32.7 1.0
CD A:LYS745 4.8 35.1 1.0
O A:HOH14 4.8 20.7 1.0
CB A:ALA743 4.8 23.4 1.0
CD1 A:LEU777 4.9 37.4 1.0
CA A:THR790 4.9 23.8 1.0

Reference:

K.Aertgeerts, R.Skene, J.Yano, B.C.Sang, H.Zou, G.Snell, A.Jennings, K.Iwamoto, N.Habuka, A.Hirokawa, T.Ishikawa, T.Tanaka, H.Miki, Y.Ohta, S.Sogabe. Structural Analysis of the Mechanism of Inhibition and Allosteric Activation of the Kinase Domain of HER2 Protein. J.Biol.Chem. V. 286 18756 2011.
ISSN: ISSN 0021-9258
PubMed: 21454582
DOI: 10.1074/JBC.M110.206193
Page generated: Sat Dec 12 10:02:59 2020

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